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PDBsum entry 2src
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Tyrosine-protein kinase PDB id
2src

 

 

 

 

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Contents
Protein chain
450 a.a. *
Ligands
ANP
Waters ×269
* Residue conservation analysis
PDB id:
2src
Name: Tyrosine-protein kinase
Title: Crystal structure of human tyrosine-protein kinasE C-src, in complex with amp-pnp
Structure: Tyrosine-protein kinase src. Chain: a. Fragment: residues 86-836, containing sh2, sh3, kinase 2 domains and c-terminal tail. Synonym: c-src, p60-src. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
1.50Å     R-factor:   0.226     R-free:   0.281
Authors: W.Xu,A.Doshi,M.Lei,M.J.Eck,S.C.Harrison
Key ref:
W.Xu et al. (1999). Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell, 3, 629-638. PubMed id: 10360179 DOI: 10.1016/S1097-2765(00)80356-1
Date:
29-Dec-98     Release date:   22-Jul-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P12931  (SRC_HUMAN) -  Proto-oncogene tyrosine-protein kinase Src from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		536 a.a.
450 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.2  - non-specific protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
 + ATP
 = O-phospho-L-tyrosyl-[protein]
Bound ligand (Het Group name = ANP)
matches with 81.25% similarity 		+ ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1016/S1097-2765(00)80356-1 Mol Cell 3:629-638 (1999)
PubMed id: 10360179  
 
 
Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
W.Xu, A.Doshi, M.Lei, M.J.Eck, S.C.Harrison.
 
  ABSTRACT  
 
Src family kinases are maintained in an assembled, inactive conformation by intramolecular interactions of their SH2 and SH3 domains. Full catalytic activity requires release of these restraints as well as phosphorylation of Tyr-416 in the activation loop. In previous structures of inactive Src kinases, Tyr-416 and flanking residues are disordered. We report here four additional c-Src structures in which this segment adopts an ordered but inhibitory conformation. The ordered activation loop forms an alpha helix that stabilizes the inactive conformation of the kinase domain, blocks the peptide substrate-binding site, and prevents Tyr-416 phosphorylation. Disassembly of the regulatory domains, induced by SH2 or SH3 ligands, or by dephosphorylation of Tyr-527, could lead to exposure and phosphorylation of Tyr-416.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Ribbon Diagram Showing the Overall Organization of Src-2The SH3 (yellow) and SH2 (green) domains coordinate the linker and phosphorylated tail segments, respectively. The tyrosine kinase domain is colored blue; AMP–PNP (red) is bound in the active site. The A loop helix packs between the N and C lobes of the kinase and sequesters Tyr-416.
Figure 7.
Figure 7. A Model for Src Activation(a) The restrained conformation of c-Src is stabilized by intramolecular interactions among the kinase domain, the SH2/SH3 domains, and the phosphorylated C-terminal tail. In this state, an inhibitory conformation of the activation loop helps disrupt the kinase active site by stabilizing a displacement of the C helix. The formation of the A loop helix, which interferes with substrate binding and protects Tyr-416 from phosphorylation, relies on a particular register of the two kinase lobes.(b) Displacement of SH2 and/or SH3 domains, either by C-terminal tail dephosphorylation or by competitive binding of optimal SH2/SH3 domain ligands, allows the kinase domain to open, disrupting the A loop helix and exposing Tyr-416 to phosphorylation.(c) Phosphorylation of Tyr-416 initiates a conformational reorganization of the whole activation loop, relieving the steric barrier for substrate binding, allowing the C-terminal helix to move back into the active site, and reconstituting a fully active tyrosine kinase.
 
  The above figures are reprinted by permission from Cell Press: Mol Cell (1999, 3, 629-638) copyright 1999.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22898541 P.K.Vogt (2012).
Retroviral oncogenes: a historical primer.
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23104056 S.Ferreira-Cerca, V.Sagar, T.Schäfer, M.Diop, A.M.Wesseling, H.Lu, E.Chai, E.Hurt, and N.Laronde-Leblanc (2012).
ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.
  Nat Struct Mol Biol, 19, 1316-1323.
PDB codes: 4gyg 4gyi
20956938 E.F.Dunn, M.Iida, R.A.Myers, D.A.Campbell, K.A.Hintz, E.A.Armstrong, C.Li, and D.L.Wheeler (2011).
Dasatinib sensitizes KRAS mutant colorectal tumors to cetuximab.
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21359199 L.P.O'Reilly, S.C.Watkins, and T.E.Smithgall (2011).
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21146412 N.E.Davey, G.Travé, and T.J.Gibson (2011).
How viruses hijack cell regulation.
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21474065 N.Jura, X.Zhang, N.F.Endres, M.A.Seeliger, T.Schindler, and J.Kuriyan (2011).
Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.
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20971646 S.S.Taylor, and A.P.Kornev (2011).
Protein kinases: evolution of dynamic regulatory proteins.
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21340460 Y.Han, N.Yuan, S.J.Zhang, J.Gao, Z.Shi, Y.B.Zhou, X.Y.Gao, and G.Q.Zhu (2011).
c-Src in paraventricular nucleus modulates sympathetic activity and cardiac sympathetic afferent reflex in renovascular hypertensive rats.
  Pflugers Arch, 461, 437-446.  
21060940 Z.B.Hill, B.G.Perera, and D.J.Maly (2011).
Bivalent inhibitors of the tyrosine kinases ABL and SRC: determinants of potency and selectivity.
  Mol Biosyst, 7, 447-456.  
20632993 C.C.Lee, Y.Jia, N.Li, X.Sun, K.Ng, E.Ambing, M.Y.Gao, S.Hua, C.Chen, S.Kim, P.Y.Michellys, S.A.Lesley, J.L.Harris, and G.Spraggon (2010).
Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain.
  Biochem J, 430, 425-437.
PDB codes: 3l9p 3lcs 3lct
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Endosomal-sorting complexes required for transport (ESCRT) pathway-dependent endosomal traffic regulates the localization of active Src at focal adhesions.
  Proc Natl Acad Sci U S A, 107, 16107-16112.  
20052711 D.J.Marcotte, Y.T.Liu, R.M.Arduini, C.A.Hession, K.Miatkowski, C.P.Wildes, P.F.Cullen, V.Hong, B.T.Hopkins, E.Mertsching, T.J.Jenkins, M.J.Romanowski, D.P.Baker, and L.F.Silvian (2010).
Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases.
  Protein Sci, 19, 429-439.
PDB codes: 3gen 3k54
20048152 G.Xi, X.Shen, and D.R.Clemmons (2010).
p66shc inhibits insulin-like growth factor-I signaling via direct binding to Src through its polyproline and Src homology 2 domains, resulting in impairment of Src kinase activation.
  J Biol Chem, 285, 6937-6951.  
20541955 K.Nika, C.Soldani, M.Salek, W.Paster, A.Gray, R.Etzensperger, L.Fugger, P.Polzella, V.Cerundolo, O.Dushek, T.Höfer, A.Viola, and O.Acuto (2010).
Constitutively active Lck kinase in T cells drives antigen receptor signal transduction.
  Immunity, 32, 766-777.  
20237289 L.Min, W.Wu, R.E.Joseph, D.B.Fulton, L.Berg, and A.H.Andreotti (2010).
Disrupting the intermolecular self-association of Itk enhances T cell signaling.
  J Immunol, 184, 4228-4235.  
20336692 M.Rabiller, M.Getlik, S.Klüter, A.Richters, S.Tückmantel, J.R.Simard, and D.Rauh (2010).
Proteus in the world of proteins: conformational changes in protein kinases.
  Arch Pharm (Weinheim), 343, 193-206.  
20584982 P.Patwardhan, and M.D.Resh (2010).
Myristoylation and membrane binding regulate c-Src stability and kinase activity.
  Mol Cell Biol, 30, 4094-4107.  
21152094 S.Dong, B.Corre, K.Nika, S.Pellegrini, and F.Michel (2010).
T cell receptor signal initiation induced by low-grade stimulation requires the cooperation of LAT in human T cells.
  PLoS One, 5, e15114.  
20421461 S.S.Taylor, and A.P.Kornev (2010).
Yet another "active" pseudokinase, Erb3.
  Proc Natl Acad Sci U S A, 107, 8047-8048.  
20209159 Y.H.Hsu, and J.A.Traugh (2010).
Reciprocally coupled residues crucial for protein kinase Pak2 activity calculated by statistical coupling analysis.
  PLoS One, 5, e9455.  
19568788 A.C.Bishop, and V.L.Chen (2009).
Brought to life: targeted activation of enzyme function with small molecules.
  J Chem Biol, 2, 1-9.  
19290920 B.B.Au-Yeung, S.Deindl, L.Y.Hsu, E.H.Palacios, S.E.Levin, J.Kuriyan, and A.Weiss (2009).
The structure, regulation, and function of ZAP-70.
  Immunol Rev, 228, 41-57.  
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Alternative splicing modulates autoinhibition and SH3 accessibility in the Src kinase Fyn.
  Mol Cell Biol, 29, 6438-6448.  
19204278 C.Hyeon, P.A.Jennings, J.A.Adams, and J.N.Onuchic (2009).
Ligand-induced global transitions in the catalytic domain of protein kinase A.
  Proc Natl Acad Sci U S A, 106, 3023-3028.  
19276677 D.L.Wheeler, M.Iida, T.J.Kruser, M.M.Nechrebecki, E.F.Dunn, E.A.Armstrong, S.Huang, and P.M.Harari (2009).
Epidermal growth factor receptor cooperates with Src family kinases in acquired resistance to cetuximab.
  Cancer Biol Ther, 8, 696-703.  
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Conformational rearrangements upon Syk auto-phosphorylation.
  Biochim Biophys Acta, 1794, 1211-1217.  
19212436 G.C.Alghisi, L.Ponsonnet, and C.Rüegg (2009).
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  PLoS ONE, 4, e4449.  
19481075 H.Kim, S.H.Rhee, C.Pothoulakis, and J.T.LaMont (2009).
Clostridium difficile toxin A binds colonocyte Src causing dephosphorylation of focal adhesion kinase and paxillin.
  Exp Cell Res, 315, 3336-3344.  
19756300 J.Dengjel, I.Kratchmarova, and B.Blagoev (2009).
Receptor tyrosine kinase signaling: a view from quantitative proteomics.
  Mol Biosyst, 5, 1112-1121.  
19833732 J.Zhao, Y.Zhang, S.S.Ithychanda, Y.Tu, K.Chen, J.Qin, and C.Wu (2009).
Migfilin interacts with Src and contributes to cell-matrix adhesion-mediated survival signaling.
  J Biol Chem, 284, 34308-34320.  
19471858 M.H.Seifert (2009).
Robust optimization of scoring functions for a target class.
  J Comput Aided Mol Des, 23, 633-644.  
19776125 M.J.Wagner, and J.R.Smiley (2009).
Herpes simplex virus requires VP11/12 to induce phosphorylation of the activation loop tyrosine (Y394) of the Src family kinase Lck in T lymphocytes.
  J Virol, 83, 12452-12461.  
19956600 M.Malakhova, I.Kurinov, K.Liu, D.Zheng, I.D'Angelo, J.H.Shim, V.Steinman, A.M.Bode, and Z.Dong (2009).
Structural diversity of the active N-terminal kinase domain of p90 ribosomal S6 kinase 2.
  PLoS One, 4, e8044.
PDB code: 3g51
18815812 M.P.Kim, S.I.Park, S.Kopetz, and G.E.Gallick (2009).
Src family kinases as mediators of endothelial permeability: effects on inflammation and metastasis.
  Cell Tissue Res, 335, 249-259.  
19620276 N.Basu, R.Bhandari, V.T.Natarajan, and S.S.Visweswariah (2009).
Cross talk between receptor guanylyl cyclase C and c-src tyrosine kinase regulates colon cancer cell cytostasis.
  Mol Cell Biol, 29, 5277-5289.  
20007378 N.Jura, Y.Shan, X.Cao, D.E.Shaw, and J.Kuriyan (2009).
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3.
  Proc Natl Acad Sci U S A, 106, 21608-21613.
PDB code: 3kex
18623061 N.K.Banavali, and B.Roux (2009).
Flexibility and charge asymmetry in the activation loop of Src tyrosine kinases.
  Proteins, 74, 378-389.  
18984583 N.K.Williams, I.S.Lucet, S.P.Klinken, E.Ingley, and J.Rossjohn (2009).
Crystal Structures of the Lyn Protein Tyrosine Kinase Domain in Its Apo- and Inhibitor-bound State.
  J Biol Chem, 284, 284-291.
PDB codes: 2zv7 2zv8 2zv9 2zva
19888460 N.M.Levinson, P.R.Visperas, and J.Kuriyan (2009).
The tyrosine kinase Csk dimerizes through Its SH3 domain.
  PLoS One, 4, e7683.  
19909368 P.E.Lapinski, J.A.Oliver, J.N.Bodie, F.Marti, and P.D.King (2009).
The T-cell-specific adapter protein family: TSAd, ALX, and SH2D4A/SH2D4B.
  Immunol Rev, 232, 240-254.  
19926274 P.Filippakopoulos, S.Müller, and S.Knapp (2009).
SH2 domains: modulators of nonreceptor tyrosine kinase activity.
  Curr Opin Struct Biol, 19, 643-649.  
19717557 Q.Qi, and A.August (2009).
The Tec family kinase Itk exists as a folded monomer in vivo.
  J Biol Chem, 284, 29882-29892.  
19150426 R.Barouch-Bentov, J.Che, C.C.Lee, Y.Yang, A.Herman, Y.Jia, A.Velentza, J.Watson, L.Sternberg, S.Kim, N.Ziaee, A.Miller, C.Jackson, M.Fujimoto, M.Young, S.Batalov, Y.Liu, M.Warmuth, T.Wiltshire, M.P.Cooke, and K.Sauer (2009).
A conserved salt bridge in the G loop of multiple protein kinases is important for catalysis and for in vivo Lyn function.
  Mol Cell, 33, 43-52.  
18761339 R.Bose, and X.Zhang (2009).
The ErbB kinase domain: structural perspectives into kinase activation and inhibition.
  Exp Cell Res, 315, 649-658.  
19164531 R.E.Iacob, T.Pene-Dumitrescu, J.Zhang, N.S.Gray, T.E.Smithgall, and J.R.Engen (2009).
Conformational disturbance in Abl kinase upon mutation and deregulation.
  Proc Natl Acad Sci U S A, 106, 1386-1391.  
19290918 R.J.Salmond, A.Filby, I.Qureshi, S.Caserta, and R.Zamoyska (2009).
T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance.
  Immunol Rev, 228, 9.  
19920178 S.Deindl, T.A.Kadlecek, X.Cao, J.Kuriyan, and A.Weiss (2009).
Stability of an autoinhibitory interface in the structure of the tyrosine kinase ZAP-70 impacts T cell receptor response.
  Proc Natl Acad Sci U S A, 106, 20699-20704.  
19427382 S.Hammond, A.Wagenknecht-Wiesner, S.L.Veatch, D.Holowka, and B.Baird (2009).
Roles for SH2 and SH3 domains in Lyn kinase association with activated FcepsilonRI in RBL mast cells revealed by patterned surface analysis.
  J Struct Biol, 168, 161-167.  
19827767 S.S.Yadav, B.J.Yeh, B.P.Craddock, W.A.Lim, and W.T.Miller (2009).
Reengineering the signaling properties of a Src family kinase.
  Biochemistry, 48, 10956-10962.  
19225111 S.Yang, N.K.Banavali, and B.Roux (2009).
Mapping the conformational transition in Src activation by cumulating the information from multiple molecular dynamics trajectories.
  Proc Natl Acad Sci U S A, 106, 3776-3781.  
19744331 T.S.Lee, W.Ma, X.Zhang, H.Kantarjian, and M.Albitar (2009).
Structural effects of clinically observed mutations in JAK2 exons 13-15: comparison with V617F and exon 12 mutations.
  BMC Struct Biol, 9, 58.  
19686639 W.Gan, S.Yang, and B.Roux (2009).
Atomistic view of the conformational activation of Src kinase using the string method with swarms-of-trajectories.
  Biophys J, 97, L8.  
19246339 Y.A.Senis, M.G.Tomlinson, S.Ellison, A.Mazharian, J.Lim, Y.Zhao, K.N.Kornerup, J.M.Auger, S.G.Thomas, T.Dhanjal, N.Kalia, J.W.Zhu, A.Weiss, and S.P.Watson (2009).
The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis.
  Blood, 113, 4942-4954.  
19406922 Y.Y.Tseng, C.Dupree, Z.J.Chen, and W.H.Li (2009).
SplitPocket: identification of protein functional surfaces and characterization of their spatial patterns.
  Nucleic Acids Res, 37, W384-W389.  
18544443 A.M.Egloff, and J.R.Grandis (2008).
Targeting epidermal growth factor receptor and SRC pathways in head and neck cancer.
  Semin Oncol, 35, 286-297.  
18282484 B.E.Turk (2008).
Understanding and exploiting substrate recognition by protein kinases.
  Curr Opin Chem Biol, 12, 4.  
18716055 B.Wu, B.Decourt, M.A.Zabidi, L.T.Wuethrich, W.H.Kim, Z.Zhou, K.MacIsaac, and D.M.Suter (2008).
Microtubule-mediated Src tyrosine kinase trafficking in neuronal growth cones.
  Mol Biol Cell, 19, 4611-4627.  
18700973 C.D.Young, E.C.Nolte, A.Lewis, N.J.Serkova, and S.M.Anderson (2008).
Activated Akt1 accelerates MMTV-c-ErbB2 mammary tumourigenesis in mice without activation of ErbB3.
  Breast Cancer Res, 10, R70.  
18765415 C.K.Sun, K.Man, K.T.Ng, J.W.Ho, Z.X.Lim, Q.Cheng, C.M.Lo, R.T.Poon, and S.T.Fan (2008).
Proline-rich tyrosine kinase 2 (Pyk2) promotes proliferation and invasiveness of hepatocellular carcinoma cells through c-Src/ERK activation.
  Carcinogenesis, 29, 2096-2105.  
18155170 D.E.Johnson (2008).
Src family kinases and the MEK/ERK pathway in the regulation of myeloid differentiation and myeloid leukemogenesis.
  Adv Enzyme Regul, 48, 98.  
18687871 E.Ozkirimli, S.S.Yadav, W.T.Miller, and C.B.Post (2008).
An electrostatic network and long-range regulation of Src kinases.
  Protein Sci, 17, 1871-1880.  
18682436 G.A.Knock, V.A.Snetkov, Y.Shaifta, S.Drndarski, J.P.Ward, and P.I.Aaronson (2008).
Role of src-family kinases in hypoxic vasoconstriction of rat pulmonary artery.
  Cardiovasc Res, 80, 453-462.  
18816084 G.Zhang, D.Fenyö, and T.A.Neubert (2008).
Screening for EphB signaling effectors using SILAC with a linear ion trap-orbitrap mass spectrometer.
  J Proteome Res, 7, 4715-4726.  
18055537 H.Fuss, W.Dubitzky, C.S.Downes, and M.J.Kurth (2008).
SRC family kinases and receptors: analysis of three activation mechanisms by dynamic systems modeling.
  Biophys J, 94, 1995-2006.  
18536014 J.D.Taylor, A.Ababou, R.R.Fawaz, C.J.Hobbs, M.A.Williams, and J.E.Ladbury (2008).
Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: implications for drug design.
  Proteins, 73, 929-940.
PDB code: 2jyq
18841497 K.Kundrapu, L.Colenberg, and R.J.Duhé (2008).
Activation loop tyrosines allow the JAK2(V617F) mutant to attain hyperactivation.
  Cell Biochem Biophys, 52, 103-112.  
17910071 M.D.Jacobs, P.R.Caron, and B.J.Hare (2008).
Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex.
  Proteins, 70, 1451-1460.
PDB code: 2pl0
18452309 S.Chen, T.P.Dumitrescu, T.E.Smithgall, and J.R.Engen (2008).
Abl N-terminal cap stabilization of SH3 domain dynamics.
  Biochemistry, 47, 5795-5803.  
18711637 S.Lu, M.Ouyang, J.Seong, J.Zhang, S.Chien, and Y.Wang (2008).
The spatiotemporal pattern of Src activation at lipid rafts revealed by diffusion-corrected FRET imaging.
  PLoS Comput Biol, 4, e1000127.  
18803405 S.S.Yadav, and W.T.Miller (2008).
The evolutionarily conserved arrangement of domains in SRC family kinases is important for substrate recognition.
  Biochemistry, 47, 10871-10880.  
18369437 S.Yang, and B.Roux (2008).
Src kinase conformational activation: thermodynamics, pathways, and mechanisms.
  PLoS Comput Biol, 4, e1000047.  
18794796 T.Pene-Dumitrescu, L.F.Peterson, N.J.Donato, and T.E.Smithgall (2008).
An inhibitor-resistant mutant of Hck protects CML cells against the antiproliferative and apoptotic effects of the broad-spectrum Src family kinase inhibitor A-419259.
  Oncogene, 27, 7055-7069.  
18328268 X.Xiong, P.Cui, S.Hossain, R.Xu, B.Warner, X.Guo, X.An, A.K.Debnath, D.Cowburn, and L.Kotula (2008).
Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1.
  Biochim Biophys Acta, 1783, 737-747.  
18984590 Y.H.Hsu, D.A.Johnson, and J.A.Traugh (2008).
Analysis of Conformational Changes during Activation of Protein Kinase Pak2 by Amide Hydrogen/Deuterium Exchange.
  J Biol Chem, 283, 36397-36405.  
17530729 A.Kumar, Y.Wang, X.Lin, G.Sun, and K.Parang (2007).
Synthesis and Evaluation of 3-Phenylpyrazolo[3,4-d]pyrimidine-Peptide Conjugates as Src Kinase Inhibitors.
  ChemMedChem, 2, 1346-1360.  
17178840 D.Adolph, N.Flach, K.Mueller, D.H.Ostareck, and A.Ostareck-Lederer (2007).
Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site.
  Mol Cell Biol, 27, 1758-1770.  
17598909 D.Tobi, and I.Bahar (2007).
Recruitment of rare 3-grams at functional sites: is this a mechanism for increasing enzyme specificity?
  BMC Bioinformatics, 8, 226.  
17890113 E.C.Jury, F.Flores-Borja, and P.S.Kabouridis (2007).
Lipid rafts in T cell signalling and disease.
  Semin Cell Dev Biol, 18, 608-615.  
17167796 G.M.Verkhivker (2007).
In silico profiling of tyrosine kinases binding specificity and drug resistance using Monte Carlo simulations with the ensembles of protein kinase crystal structures.
  Biopolymers, 85, 333-348.  
17173284 G.M.Verkhivker (2007).
Computational proteomics of biomolecular interactions in the sequence and structure space of the tyrosine kinome: deciphering the molecular basis of the kinase inhibitors selectivity.
  Proteins, 66, 912-929.  
17671639 H.Zhang, A.Berezov, Q.Wang, G.Zhang, J.Drebin, R.Murali, and M.I.Greene (2007).
ErbB receptors: from oncogenes to targeted cancer therapies.
  J Clin Invest, 117, 2051-2058.  
17585314 J.A.Ubersax, and J.E.Ferrell (2007).
Mechanisms of specificity in protein phosphorylation.
  Nat Rev Mol Cell Biol, 8, 530-541.  
17292838 J.Eswaran, W.H.Lee, J.E.Debreczeni, P.Filippakopoulos, A.Turnbull, O.Fedorov, S.W.Deacon, J.R.Peterson, and S.Knapp (2007).
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.
  Structure, 15, 201-213.
PDB codes: 2bva 2c30 2cdz 2f57
17521420 J.L.Jiménez, B.Hegemann, J.R.Hutchins, J.M.Peters, and R.Durbin (2007).
A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database.
  Genome Biol, 8, R90.  
17961998 J.Liu, and J.I.Shapiro (2007).
Regulation of sodium pump endocytosis by cardiotonic steroids: Molecular mechanisms and physiological implications.
  Pathophysiology, 14, 171-181.  
17412687 J.Xu, X.H.Bai, M.Lodyga, B.Han, H.Xiao, S.Keshavjee, J.Hu, H.Zhang, B.B.Yang, and M.Liu (2007).
XB130, a novel adaptor protein for signal transduction.
  J Biol Chem, 282, 16401-16412.  
  17200208 J.Zhang, S.Kalyankrishna, M.Wislez, N.Thilaganathan, B.Saigal, W.Wei, L.Ma, I.I.Wistuba, F.M.Johnson, and J.M.Kurie (2007).
SRC-family kinases are activated in non-small cell lung cancer and promote the survival of epidermal growth factor receptor-dependent cell lines.
  Am J Pathol, 170, 366-376.  
17921256 L.Li, K.Hisamoto, K.H.Kim, M.P.Haynes, P.M.Bauer, A.Sanjay, M.Collinge, R.Baron, W.C.Sessa, and J.R.Bender (2007).
Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation.
  Proc Natl Acad Sci U S A, 104, 16468-16473.  
17088251 L.S.Chaturvedi, H.M.Marsh, X.Shang, Y.Zheng, and M.D.Basson (2007).
Repetitive deformation activates focal adhesion kinase and ERK mitogenic signals in human Caco-2 intestinal epithelial cells through Src and Rac1.
  J Biol Chem, 282, 14-28.  
17355866 M.A.Seeliger, B.Nagar, F.Frank, X.Cao, M.N.Henderson, and J.Kuriyan (2007).
c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty.
  Structure, 15, 299-311.
PDB code: 2oiq
17159994 M.Faller, M.Matsunaga, S.Yin, J.A.Loo, and F.Guo (2007).
Heme is involved in microRNA processing.
  Nat Struct Mol Biol, 14, 23-29.  
17380483 N.K.Banavali, and B.Roux (2007).
Anatomy of a structural pathway for activation of the catalytic domain of Src kinase Hck.
  Proteins, 67, 1096-1112.  
17115885 P.Chiarugi, and F.Buricchi (2007).
Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications.
  Antioxid Redox Signal, 9, 1.  
17173075 R.C.Ishizawar, T.Miyake, and S.J.Parsons (2007).
c-Src modulates ErbB2 and ErbB3 heterocomplex formation and function.
  Oncogene, 26, 3503-3510.  
17919561 R.R.Hodges, Y.Horikawa, J.D.Rios, M.A.Shatos, and D.A.Dartt (2007).
Effect of protein kinase C and Ca(2+) on p42/p44 MAPK, Pyk2, and Src activation in rat conjunctival goblet cells.
  Exp Eye Res, 85, 836-844.  
17327393 S.Chen, S.Brier, T.E.Smithgall, and J.R.Engen (2007).
The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.
  Protein Sci, 16, 572-581.  
17512407 S.Deindl, T.A.Kadlecek, T.Brdicka, X.Cao, A.Weiss, and J.Kuriyan (2007).
Structural basis for the inhibition of tyrosine kinase activity of ZAP-70.
  Cell, 129, 735-746.
PDB code: 2ozo
17719722 S.S.Yadav, and W.T.Miller (2007).
Cooperative activation of Src family kinases by SH3 and SH2 ligands.
  Cancer Lett, 257, 116-123.  
17164530 S.W.Cowan-Jacob, G.Fendrich, A.Floersheimer, P.Furet, J.Liebetanz, G.Rummel, P.Rheinberger, M.Centeleghe, D.Fabbro, and P.W.Manley (2007).
Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia.
  Acta Crystallogr D Biol Crystallogr, 63, 80-93.
PDB codes: 2hyy 2hz0 2hz4 2hzi 2hzn
17686471 T.A.Garrett, J.D.Van Buul, and K.Burridge (2007).
VEGF-induced Rac1 activation in endothelial cells is regulated by the guanine nucleotide exchange factor Vav2.
  Exp Cell Res, 313, 3285-3297.  
17583354 T.Furukawa, and J.Kurokawa (2007).
Regulation of cardiac ion channels via non-genomic action of sex steroid hormones: implication for the gender difference in cardiac arrhythmias.
  Pharmacol Ther, 115, 106-115.  
16803889 A.Marx, C.Nugoor, J.Müller, S.Panneerselvam, T.Timm, M.Bilang, E.Mylonas, D.I.Svergun, E.M.Mandelkow, and E.Mandelkow (2006).
Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2.
  J Biol Chem, 281, 27586-27599.
PDB code: 2hak
17095602 A.P.Kornev, N.M.Haste, S.S.Taylor, and L.F.Eyck (2006).
Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism.
  Proc Natl Acad Sci U S A, 103, 17783-17788.  
16600665 C.L.Elsegood, Y.Zhuo, G.A.Wesolowski, J.A.Hamilton, G.A.Rodan, and l.e. .T.Duong (2006).
M-CSF induces the stable interaction of cFms with alphaVbeta3 integrin in osteoclasts.
  Int J Biochem Cell Biol, 38, 1518-1529.  
16492148 D.Dalgarno, T.Stehle, S.Narula, P.Schelling, M.R.van Schravendijk, S.Adams, L.Andrade, J.Keats, M.Ram, L.Jin, T.Grossman, I.MacNeil, C.Metcalf, W.Shakespeare, Y.Wang, T.Keenan, R.Sundaramoorthi, R.Bohacek, M.Weigele, and T.Sawyer (2006).
Structural basis of Src tyrosine kinase inhibition with a new class of potent and selective trisubstituted purine-based compounds.
  Chem Biol Drug Des, 67, 46-57.
PDB codes: 2bdf 2bdj
16597828 E.Ozkirimli, and C.B.Post (2006).
Src kinase activation: A switched electrostatic network.
  Protein Sci, 15, 1051-1062.  
16899073 H.T.Le, L.Maksumova, J.Wang, and C.J.Pallen (2006).
Reduced NMDA receptor tyrosine phosphorylation in PTPalpha-deficient mouse synaptosomes is accompanied by inhibition of four src family kinases and Pyk2: an upstream role for PTPalpha in NMDA receptor regulation.
  J Neurochem, 98, 1798-1809.  
16891373 H.X.Zhou (2006).
Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains.
  Biophys J, 91, 3170-3181.  
16322569 J.M.Hochrein, E.C.Lerner, A.P.Schiavone, T.E.Smithgall, and J.R.Engen (2006).
An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry.
  Protein Sci, 15, 65-73.  
16371504 J.Qi, J.Wang, O.Romanyuk, and C.H.Siu (2006).
Involvement of Src family kinases in N-cadherin phosphorylation and beta-catenin dissociation during transendothelial migration of melanoma cells.
  Mol Biol Cell, 17, 1261-1272.  
16809767 J.Yue, and J.E.Ferrell (2006).
Mechanistic studies of the mitotic activation of Mos.
  Mol Cell Biol, 26, 5300-5309.  
16407246 K.Hattori, S.Uchino, T.Isosaka, M.Maekawa, M.Iyo, T.Sato, S.Kohsaka, T.Yagi, and S.Yuasa (2006).
Fyn is required for haloperidol-induced catalepsy in mice.
  J Biol Chem, 281, 7129-7135.  
16507567 M.Chen, S.C.Chen, and C.J.Pallen (2006).
Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration.
  J Biol Chem, 281, 11972-11980.  
16640460 N.M.Levinson, O.Kuchment, K.Shen, M.A.Young, M.Koldobskiy, M.Karplus, P.A.Cole, and J.Kuriyan (2006).
A Src-like inactive conformation in the abl tyrosine kinase domain.
  PLoS Biol, 4, e144.
PDB codes: 2g1t 2g2f 2g2h 2g2i
17079130 P.Pellicena, and J.Kuriyan (2006).
Protein-protein interactions in the allosteric regulation of protein kinases.
  Curr Opin Struct Biol, 16, 702-709.  
16611580 P.S.Kabouridis (2006).
Lipid rafts in T cell receptor signalling .
  Mol Membr Biol, 23, 49-57.  
16633924 T.Miyazaki, S.Tanaka, A.Sanjay, and R.Baron (2006).
The role of c-Src kinase in the regulation of osteoclast function.
  Mod Rheumatol, 16, 68-74.  
16777603 X.Zhang, J.Gureasko, K.Shen, P.A.Cole, and J.Kuriyan (2006).
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.
  Cell, 125, 1137-1149.
PDB codes: 2gs2 2gs6 2gs7
16291744 Z.Zhang, S.Y.Lin, B.G.Neel, and B.Haimovich (2006).
Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration.
  J Biol Chem, 281, 1746-1754.  
15709962 D.P.Edwards (2005).
Regulation of signal transduction pathways by estrogen and progesterone.
  Annu Rev Physiol, 67, 335-376.  
16210316 E.C.Lerner, R.P.Trible, A.P.Schiavone, J.M.Hochrein, J.R.Engen, and T.E.Smithgall (2005).
Activation of the Src family kinase Hck without SH3-linker release.
  J Biol Chem, 280, 40832-40837.  
16244704 E.D.Scheeff, and P.E.Bourne (2005).
Structural evolution of the protein kinase-like superfamily.
  PLoS Comput Biol, 1, e49.  
15618230 G.H.Iyer, M.J.Moore, and S.S.Taylor (2005).
Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase.
  J Biol Chem, 280, 8800-8807.  
15842360 H.Kato, S.Honda, H.Yoshida, H.Kashiwagi, M.Shiraga, N.Honma, Y.Kurata, and Y.Tomiyama (2005).
SHPS-1 negatively regulates integrin alphaIIbbeta3 function through CD47 without disturbing FAK phosphorylation.
  J Thromb Haemost, 3, 763-774.  
15557335 M.H.Schmidt, I.Dikic, and O.Bögler (2005).
Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities.
  J Biol Chem, 280, 3414-3425.  
15893667 M.Lei, M.A.Robinson, and S.C.Harrison (2005).
The active conformation of the PAK1 kinase domain.
  Structure, 13, 769-778.
PDB codes: 1yhv 1yhw
15611931 N.Hosoya, Y.Qiao, A.Hangaishi, L.Wang, Y.Nannya, M.Sanada, M.Kurokawa, S.Chiba, H.Hirai, and S.Ogawa (2005).
Identification of a SRC-like tyrosine kinase gene, FRK, fused with ETV6 in a patient with acute myelogenous leukemia carrying a t(6;12)(q21;p13) translocation.
  Genes Chromosomes Cancer, 42, 269-279.  
16271895 N.K.Banavali, and B.Roux (2005).
The N-terminal end of the catalytic domain of SRC kinase Hck is a conformational switch implicated in long-range allosteric regulation.
  Structure, 13, 1715-1723.  
16154907 P.Ozegbe, Y.Chernajovsky, and P.S.Kabouridis (2005).
Regulation of expression and function of Lck tyrosine kinase by high cell density.
  Mol Membr Biol, 22, 363-372.  
15939018 S.W.Cowan-Jacob, G.Fendrich, P.W.Manley, W.Jahnke, D.Fabbro, J.Liebetanz, and T.Meyer (2005).
The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation.
  Structure, 13, 861-871.
PDB code: 1y57
15579470 W.Li, C.Marshall, L.Mei, L.Dzubow, C.Schmults, M.Dans, and J.Seykora (2005).
Srcasm modulates EGF and Src-kinase signaling in keratinocytes.
  J Biol Chem, 280, 6036-6046.  
15326593 A.M.Aronov, and G.W.Bemis (2004).
A minimalist approach to fragment-based ligand design using common rings and linkers: application to kinase inhibitors.
  Proteins, 57, 36-50.  
15485829 B.Han, X.H.Bai, M.Lodyga, J.Xu, B.B.Yang, S.Keshavjee, M.Post, and M.Liu (2004).
Conversion of mechanical force into biochemical signaling.
  J Biol Chem, 279, 54793-54801.  
15141006 B.Kwiatkowski, S.Y.Chen, and W.H.Schubach (2004).
CKII site in Epstein-Barr virus nuclear protein 2 controls binding to hSNF5/Ini1 and is important for growth transformation.
  J Virol, 78, 6067-6072.  
15292208 B.Olszewska-Pazdrak, C.M.Townsend, and M.R.Hellmich (2004).
Agonist-independent activation of Src tyrosine kinase by a cholecystokinin-2 (CCK2) receptor splice variant.
  J Biol Chem, 279, 40400-40404.  
14625311 J.Felberg, D.C.Lefebvre, M.Lam, Y.Wang, D.H.Ng, D.Birkenhead, J.L.Cross, and P.Johnson (2004).
Subdomain X of the kinase domain of Lck binds CD45 and facilitates dephosphorylation.
  J Biol Chem, 279, 3455-3462.  
15556675 J.P.Ward, G.A.Knock, V.A.Snetkov, and P.I.Aaronson (2004).
Protein kinases in vascular smooth muscle tone--role in the pulmonary vasculature and hypoxic pulmonary vasoconstriction.
  Pharmacol Ther, 104, 207-231.  
15173188 K.Kasahara, Y.Nakayama, K.Ikeda, Y.Fukushima, D.Matsuda, S.Horimoto, and N.Yamaguchi (2004).
Trafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domain.
  J Cell Biol, 165, 641-652.  
15345216 L.Duan, A.L.Reddi, A.Ghosh, M.Dimri, and H.Band (2004).
The Cbl family and other ubiquitin ligases: destructive forces in control of antigen receptor signaling.
  Immunity, 21, 7.  
15143068 M.S.Toledo, E.Suzuki, K.Handa, and S.Hakomori (2004).
Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13.
  J Biol Chem, 279, 34655-34664.  
15034556 M.W.Salter, and L.V.Kalia (2004).
Src kinases: a hub for NMDA receptor regulation.
  Nat Rev Neurosci, 5, 317-328.  
15031291 R.C.Ishizawar, D.A.Tice, T.Karaoli, and S.J.Parsons (2004).
The C terminus of c-Src inhibits breast tumor cell growth by a kinase-independent mechanism.
  J Biol Chem, 279, 23773-23781.  
15380511 R.Ishizawar, and S.J.Parsons (2004).
c-Src and cooperating partners in human cancer.
  Cancer Cell, 6, 209-214.  
14718917 S.C.Harrison (2004).
Whither structural biology?
  Nat Struct Mol Biol, 11, 12-15.  
14739300 T.Miyazaki, A.Sanjay, L.Neff, S.Tanaka, W.C.Horne, and R.Baron (2004).
Src kinase activity is essential for osteoclast function.
  J Biol Chem, 279, 17660-17666.  
15258137 T.Prince, and R.L.Matts (2004).
Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37.
  J Biol Chem, 279, 39975-39981.  
15572780 T.R.Schneider (2004).
Domain identification by iterative analysis of error-scaled difference distance matrices.
  Acta Crystallogr D Biol Crystallogr, 60, 2269-2275.  
12697812 B.H.Ahn, S.Y.Kim, E.H.Kim, K.S.Choi, T.K.Kwon, Y.H.Lee, J.S.Chang, M.S.Kim, Y.H.Jo, and D.S.Min (2003).
Transmodulation between phospholipase D and c-Src enhances cell proliferation.
  Mol Cell Biol, 23, 3103-3115.  
12654251 B.Nagar, O.Hantschel, M.A.Young, K.Scheffzek, D.Veach, W.Bornmann, B.Clarkson, G.Superti-Furga, and J.Kuriyan (2003).
Structural basis for the autoinhibition of c-Abl tyrosine kinase.
  Cell, 112, 859-871.
PDB codes: 1opj 1opk 1opl
12695509 C.Thornton, R.Yaka, S.Dinh, and D.Ron (2003).
H-Ras modulates N-methyl-D-aspartate receptor function via inhibition of Src tyrosine kinase activity.
  J Biol Chem, 278, 23823-23829.  
12473651 J.Zhou, J.Scholes, and J.T.Hsieh (2003).
Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in normal prostatic epithelium and cancer.
  J Biol Chem, 278, 6936-6941.  
12670404 K.Alexandropoulos, L.T.Donlin, L.Xing, and A.G.Regelmann (2003).
Sin: good or bad? A T lymphocyte perspective.
  Immunol Rev, 192, 181-195.  
12709437 K.Maeno, K.Sada, S.Kyo, S.M.Miah, K.Kawauchi-Kamata, X.Qu, Y.Shi, and H.Yamamura (2003).
Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase.
  J Biol Chem, 278, 24912-24920.  
12748290 K.Q.Tanis, D.Veach, H.S.Duewel, W.G.Bornmann, and A.J.Koleske (2003).
Two distinct phosphorylation pathways have additive effects on Abl family kinase activation.
  Mol Cell Biol, 23, 3884-3896.  
12654249 M.Azam, R.R.Latek, and G.Q.Daley (2003).
Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL.
  Cell, 112, 831-843.  
12499371 M.J.Moore, J.A.Adams, and S.S.Taylor (2003).
Structural basis for peptide binding in protein kinase A. Role of glutamic acid 203 and tyrosine 204 in the peptide-positioning loop.
  J Biol Chem, 278, 10613-10618.  
12464621 M.Kong, C.Mounier, V.Dumas, and B.I.Posner (2003).
Epidermal growth factor-induced DNA synthesis. Key role for Src phosphorylation of the docking protein Gab2.
  J Biol Chem, 278, 5837-5844.  
12554652 M.Selbach, S.Moese, R.Hurwitz, C.R.Hauck, T.F.Meyer, and S.Backert (2003).
The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation.
  EMBO J, 22, 515-528.  
12496276 O.Cen, M.M.Gorska, S.J.Stafford, S.Sur, and R.Alam (2003).
Identification of UNC119 as a novel activator of SRC-type tyrosine kinases.
  J Biol Chem, 278, 8837-8845.  
12624102 P.Rudrabhatla, and R.Rajasekharan (2003).
Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity.
  J Biol Chem, 278, 17328-17335.  
12686600 P.Saharinen, M.Vihinen, and O.Silvennoinen (2003).
Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in its pseudokinase domain.
  Mol Biol Cell, 14, 1448-1459.  
12654240 S.C.Harrison (2003).
Variation on an Src-like theme.
  Cell, 112, 737-740.  
12589038 S.Niu, H.Xie, and E.E.Marcantonio (2003).
Integrin-mediated tyrosine phosphorylation of Shc in T cells is regulated by protein kinase C-dependent phosphorylations of Lck.
  Mol Biol Cell, 14, 349-360.  
12779336 S.S.Martin, V.C.Chu, and E.Baldwin (2003).
Modulation of the active complex assembly and turnover rate by protein-DNA interactions in Cre-LoxP recombination.
  Biochemistry, 42, 6814-6826.
PDB code: 1ma7
12548283 T.A.Young, B.Delagoutte, J.A.Endrizzi, A.M.Falick, and T.Alber (2003).
Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases.
  Nat Struct Biol, 10, 168-174.
PDB code: 1mru
12517337 X.Huang, M.Begley, K.A.Morgenstern, Y.Gu, P.Rose, H.Zhao, and X.Zhu (2003).
Crystal structure of an inactive Akt2 kinase domain.
  Structure, 11, 21-30.
PDB codes: 1mrv 1mry
11940607 A.Obergfell, K.Eto, A.Mocsai, C.Buensuceso, S.L.Moores, J.S.Brugge, C.A.Lowell, and S.J.Shattil (2002).
Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.
  J Cell Biol, 157, 265-275.  
11976726 E.C.Lerner, and T.E.Smithgall (2002).
SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo.
  Nat Struct Biol, 9, 365-369.  
12391316 F.Du, F.Navarro-Garcia, Z.Xia, T.Tasaki, and A.Varshavsky (2002).
Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.
  Proc Natl Acad Sci U S A, 99, 14110-14115.  
12203728 J.L.Walker, L.Zhang, and A.S.Menko (2002).
Transition between proliferation and differentiation for lens epithelial cells is regulated by Src family kinases.
  Dev Dyn, 224, 361-372.  
12221082 J.M.Schmitt, and P.J.Stork (2002).
Galpha and Gbeta gamma require distinct Src-dependent pathways to activate Rap1 and Ras.
  J Biol Chem, 277, 43024-43032.  
12191607 K.Parang, and P.A.Cole (2002).
Designing bisubstrate analog inhibitors for protein kinases.
  Pharmacol Ther, 93, 145-157.  
11841936 L.A.Witucki, X.Huang, K.Shah, Y.Liu, S.Kyin, M.J.Eck, and K.M.Shokat (2002).
Mutant tyrosine kinases with unnatural nucleotide specificity retain the structure and phospho-acceptor specificity of the wild-type enzyme.
  Chem Biol, 9, 25-33.
PDB code: 1ksw
11809811 L.Li, M.Okura, and A.Imamoto (2002).
Focal adhesions require catalytic activity of Src family kinases to mediate integrin-matrix adhesion.
  Mol Cell Biol, 22, 1203-1217.  
12142282 M.A.Pufall, and B.J.Graves (2002).
Autoinhibitory domains: modular effectors of cellular regulation.
  Annu Rev Cell Dev Biol, 18, 421-462.  
11994738 M.B.Yaffe (2002).
Phosphotyrosine-binding domains in signal transduction.
  Nat Rev Mol Cell Biol, 3, 177-186.  
12020799 M.C.Frame (2002).
Src in cancer: deregulation and consequences for cell behaviour.
  Biochim Biophys Acta, 1602, 114-130.  
12015977 M.Huse, and J.Kuriyan (2002).
The conformational plasticity of protein kinases.
  Cell, 109, 275-282.  
11875070 M.K.Abe, M.P.Saelzler, R.Espinosa, K.T.Kahle, M.B.Hershenson, M.M.Le Beau, and M.R.Rosner (2002).
ERK8, a new member of the mitogen-activated protein kinase family.
  J Biol Chem, 277, 16733-16743.  
12191603 R.A.Engh, and D.Bossemeyer (2002).
Structural aspects of protein kinase control-role of conformational flexibility.
  Pharmacol Ther, 93, 99.  
12244095 S.J.Schreiner, A.P.Schiavone, and T.E.Smithgall (2002).
Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain.
  J Biol Chem, 277, 45680-45687.  
11306297 A.C.Bishop, O.Buzko, and K.M.Shokat (2001).
Magic bullets for protein kinases.
  Trends Cell Biol, 11, 167-172.  
  11602604 A.Derrien, and K.M.Druey (2001).
RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation.
  J Biol Chem, 276, 48532-48538.  
11598120 A.J.Ablooglu, M.Frankel, E.Rusinova, J.B.Ross, and R.A.Kohanski (2001).
Multiple activation loop conformations and their regulatory properties in the insulin receptor's kinase domain.
  J Biol Chem, 276, 46933-46940.  
11149930 A.Sanjay, A.Houghton, L.Neff, E.DiDomenico, C.Bardelay, E.Antoine, J.Levy, J.Gailit, D.Bowtell, W.C.Horne, and R.Baron (2001).
Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility.
  J Cell Biol, 152, 181-195.  
11774228 A.Y.Ting, K.Witte, K.Shah, B.Kraybill, K.M.Shokat, and P.G.Schultz (2001).
Phage-display evolution of tyrosine kinases with altered nucleotide specificity.
  Biopolymers, 60, 220-228.  
11583620 C.H.Lin, B.J.Hare, G.Wagner, S.C.Harrison, T.Maniatis, and E.Fraenkel (2001).
A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.
  Mol Cell, 8, 581-590.
PDB code: 1jjs
11376432 D.J.Dunican, and P.Doherty (2001).
Designing cell-permeant phosphopeptides to modulate intracellular signaling pathways.
  Biopolymers, 60, 45-60.  
  11713347 D.S.Goodsell (2001).
The molecular perspective: the Src oncogene.
  Stem Cells, 19, 553-555.  
11714930 L.H.Weaver, K.Kwon, D.Beckett, and B.W.Matthews (2001).
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
  Protein Sci, 10, 2618-2622.
PDB codes: 1k67 1k69
11301007 M.A.Young, S.Gonfloni, G.Superti-Furga, B.Roux, and J.Kuriyan (2001).
Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation.
  Cell, 105, 115-126.  
11354004 M.Miller, K.Ginalski, B.Lesyng, N.Nakaigawa, L.Schmidt, and B.Zbar (2001).
Structural basis of oncogenic activation caused by point mutations in the kinase domain of the MET proto-oncogene: modeling studies.
  Proteins, 44, 32-43.  
11391566 N.V.Prabhu, S.A.Siddiqui, J.S.McMurray, and B.M.Pettitt (2001).
Structural basis for the activity of pp60(c-src) protein tyrosine kinase inhibitors.
  Biopolymers, 59, 167-179.  
11545730 V.Boonyaratanakornkit, M.P.Scott, V.Ribon, L.Sherman, S.M.Anderson, J.L.Maller, W.T.Miller, and D.P.Edwards (2001).
Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases.
  Mol Cell, 8, 269-280.  
11031232 A.Bretscher, D.Chambers, R.Nguyen, and D.Reczek (2000).
ERM-Merlin and EBP50 protein families in plasma membrane organization and function.
  Annu Rev Cell Dev Biol, 16, 113-143.  
11032808 A.Migliaccio, G.Castoria, M.Di Domenico, A.de Falco, A.Bilancio, M.Lombardi, M.V.Barone, D.Ametrano, M.S.Zannini, C.Abbondanza, and F.Auricchio (2000).
Steroid-induced androgen receptor-oestradiol receptor beta-Src complex triggers prostate cancer cell proliferation.
  EMBO J, 19, 5406-5417.  
10958675 A.W.Lee, and D.J.States (2000).
Both src-dependent and -independent mechanisms mediate phosphatidylinositol 3-kinase regulation of colony-stimulating factor 1-activated mitogen-activated protein kinases in myeloid progenitors.
  Mol Cell Biol, 20, 6779-6798.  
  11106171 D.A.Henriques, J.E.Ladbury, and R.M.Jackson (2000).
Comparison of binding energies of SrcSH2-phosphotyrosyl peptides with structure-based prediction using surface area based empirical parameterization.
  Protein Sci, 9, 1975-1985.  
11106755 D.Durocher, I.A.Taylor, D.Sarbassova, L.F.Haire, S.L.Westcott, S.P.Jackson, S.J.Smerdon, and M.B.Yaffe (2000).
The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.
  Mol Cell, 6, 1169-1182.
PDB code: 1g6g
10995582 D.R.Alexander (2000).
The CD45 tyrosine phosphatase: a positive and negative regulator of immune cell function.
  Semin Immunol, 12, 349-359.  
10958693 G.Scholz, S.D.Hartson, K.Cartledge, N.Hall, J.Shao, A.R.Dunn, and R.L.Matts (2000).
p50(Cdc37) can buffer the temperature-sensitive properties of a mutant of Hck.
  Mol Cell Biol, 20, 6984-6995.  
10805770 J.A.Endrizzi, P.T.Beernink, T.Alber, and H.K.Schachman (2000).
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
  Proc Natl Acad Sci U S A, 97, 5077-5082.
PDB code: 1ekx
11057895 J.Schlessinger (2000).
Cell signaling by receptor tyrosine kinases.
  Cell, 103, 211-225.  
10809752 K.Iwabuchi, Y.Zhang, K.Handa, D.A.Withers, P.Sinaÿ, and S.Hakomori (2000).
Reconstitution of membranes simulating "glycosignaling domain" and their susceptibility to lyso-GM3.
  J Biol Chem, 275, 15174-15181.  
10971656 K.Sato, M.Kimoto, M.Kakumoto, D.Horiuchi, T.Iwasaki, A.A.Tokmakov, and Y.Fukami (2000).
Adaptor protein Shc undergoes translocation and mediates up-regulation of the tyrosine kinase c-Src in EGF-stimulated A431 cells.
  Genes Cells, 5, 749-764.  
10975528 M.Lei, W.Lu, W.Meng, M.C.Parrini, M.J.Eck, B.J.Mayer, and S.C.Harrison (2000).
Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch.
  Cell, 102, 387-397.
PDB code: 1f3m
11087407 M.P.Scott, and W.T.Miller (2000).
A peptide model system for processive phosphorylation by Src family kinases.
  Biochemistry, 39, 14531-14537.  
10644735 M.Porter, T.Schindler, J.Kuriyan, and W.T.Miller (2000).
Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand.
  J Biol Chem, 275, 2721-2726.  
11121839 M.Susva, M.Missbach, and J.Green (2000).
Src inhibitors: drugs for the treatment of osteoporosis, cancer or both?
  Trends Pharmacol Sci, 21, 489-495.  
10679375 R.S.Gokhale, and C.Khosla (2000).
Role of linkers in communication between protein modules.
  Curr Opin Chem Biol, 4, 22-27.  
10966463 S.R.Hubbard, and J.H.Till (2000).
Protein tyrosine kinase structure and function.
  Annu Rev Biochem, 69, 373-398.  
10647936 T.Hunter (2000).
Signaling--2000 and beyond.
  Cell, 100, 113-127.  
10988075 T.Schindler, W.Bornmann, P.Pellicena, W.T.Miller, B.Clarkson, and J.Kuriyan (2000).
Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
  Science, 289, 1938-1942.
PDB code: 1fpu
11007482 Y.C.Ma, J.Huang, S.Ali, W.Lowry, and X.Y.Huang (2000).
Src tyrosine kinase is a novel direct effector of G proteins.
  Cell, 102, 635-646.  
10611675 A.Sali, and J.Kuriyan (1999).
Challenges at the frontiers of structural biology.
  Trends Cell Biol, 9, M20-M24.  
10570142 K.F.Harris, I.Shoji, E.M.Cooper, S.Kumar, H.Oda, and P.M.Howley (1999).
Ubiquitin-mediated degradation of active Src tyrosine kinase.
  Proc Natl Acad Sci U S A, 96, 13738-13743.  
10360180 T.Schindler, F.Sicheri, A.Pico, A.Gazit, A.Levitzki, and J.Kuriyan (1999).
Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor.
  Mol Cell, 3, 639-648.
PDB code: 1qcf
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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