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PDBsum entry 1fyn
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Transferase PDB id
1fyn

 

 

 

 

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Contents
Protein chain
62 a.a. *
Ligands
PRO-PRO-ALA-TYR-
PRO-PRO-PRO-PRO-
VAL-PRO
Waters ×37
* Residue conservation analysis
PDB id:
1fyn
Name: Transferase
Title: Phosphotransferase
Structure: Phosphotransferase fyn. Chain: a. Fragment: sh3 domain. Synonym: proto-oncogene tyrosine kinase. Engineered: yes. 3bp-2. Chain: b. Engineered: yes. Other_details: synthetic peptide (ppaypppppvp)
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21 de3. Gene: fyn tyrosine kinase. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.30Å     R-factor:   0.234    
Authors: A.Musacchio,M.Saraste,M.Wilmanns
Key ref: A.Musacchio et al. (1994). High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat Struct Biol, 1, 546-551. PubMed id: 7664083
Date:
17-May-95     Release date:   08-Nov-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06241  (FYN_HUMAN) -  Tyrosine-protein kinase Fyn from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		537 a.a.
62 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]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Nat Struct Biol 1:546-551 (1994)
PubMed id: 7664083  
 
 
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
A.Musacchio, M.Saraste, M.Wilmanns.
 
  ABSTRACT  
 
Src-homology 3 (SH3) domains bind to proline-rich motifs in target proteins. We have determined high-resolution crystal structures of the complexes between the SH3 domains of Abl and Fyn tyrosine kinases, and two ten-residue proline-rich peptides derived from the SH3-binding proteins 3BP-1 and 3BP-2. The X-ray data show that the basic mode of binding of both proline-rich peptides is the same. Peptides are bound over their entire length and interact with three major sites on the SH3 molecules by both hydrogen-bonding and van der Waals contacts. Residues 4-10 of the peptide adopt the conformation of a left-handed polyproline helix type II. Binding of the proline at position 2 requires a kink at the non-proline position 3.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19906645 A.Palencia, A.Camara-Artigas, M.T.Pisabarro, J.C.Martinez, and I.Luque (2010).
Role of interfacial water molecules in proline-rich ligand recognition by the Src homology 3 domain of Abl.
  J Biol Chem, 285, 2823-2833.
PDB codes: 3eg0 3eg1 3eg2 3eg3 3egu
19921743 C.Rubini, P.Ruzza, M.R.Spaller, G.Siligardi, R.Hussain, D.G.Udugamasooriya, M.Bellanda, S.Mammi, A.Borgogno, A.Calderan, L.Cesaro, A.M.Brunati, and A.Donella-Deana (2010).
Recognition of lysine-rich peptide ligands by murine cortactin SH3 domain: CD, ITC, and NMR studies.
  Biopolymers, 94, 298-306.  
20467438 M.I.Arbuckle, N.H.Komiyama, A.Delaney, M.Coba, E.M.Garry, R.Rosie, A.J.Allchorne, L.H.Forsyth, M.Bence, H.J.Carlisle, T.J.O'Dell, R.Mitchell, S.M.Fleetwood-Walker, and S.G.Grant (2010).
The SH3 domain of postsynaptic density 95 mediates inflammatory pain through phosphatidylinositol-3-kinase recruitment.
  EMBO Rep, 11, 473-478.  
21098279 O.Aitio, M.Hellman, A.Kazlauskas, D.F.Vingadassalom, J.M.Leong, K.Saksela, and P.Permi (2010).
Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly.
  Proc Natl Acad Sci U S A, 107, 21743-21748.
PDB code: 2kxc
19712106 A.Stein, R.A.Pache, P.Bernadó, M.Pons, and P.Aloy (2009).
Dynamic interactions of proteins in complex networks: a more structured view.
  FEBS J, 276, 5390-5405.  
19432457 S.P.Edmondson, J.Turri, K.Smith, A.Clark, and J.W.Shriver (2009).
Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricus.
  Biochemistry, 48, 5553-5562.  
19023120 T.Hou, Z.Xu, W.Zhang, W.A.McLaughlin, D.A.Case, Y.Xu, and W.Wang (2009).
Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains.
  Mol Cell Proteomics, 8, 639-649.  
  19342780 Z.Shi, N.Liang, W.Xu, K.Li, G.Sheng, J.Liu, A.Xu, X.J.Li, and D.Wu (2009).
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 361-363.  
18275817 R.A.Robinson, X.Lu, E.Y.Jones, and C.Siebold (2008).
Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73.
  Structure, 16, 259-268.
PDB code: 2vge
18721137 S.A.Solheim, E.Petsalaki, A.J.Stokka, R.B.Russell, K.Taskén, and T.Berge (2008).
Interactions between the Fyn SH3-domain and adaptor protein Cbp/PAG derived ligands, effects on kinase activity and affinity.
  FEBS J, 275, 4863-4874.  
17452790 A.Cámara-Artigas, A.Palencia, J.C.Martínez, I.Luque, J.A.Gavira, and J.M.García-Ruiz (2007).
Crystallization by capillary counter-diffusion and structure determination of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with a high-affinity peptide ligand.
  Acta Crystallogr D Biol Crystallogr, 63, 646-652.
PDB code: 2o88
17367393 B.Bommarius, D.Maxwell, A.Swimm, S.Leung, A.Corbett, W.Bornmann, and D.Kalman (2007).
Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation.
  Mol Microbiol, 63, 1748-1768.  
17698610 D.E.Shvartsman, J.C.Donaldson, B.Diaz, O.Gutman, G.S.Martin, and Y.I.Henis (2007).
Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.
  J Cell Biol, 178, 675-686.  
17164526 J.Gruber, A.Zawaira, R.Saunders, C.P.Barrett, and M.E.Noble (2007).
Computational analyses of the surface properties of protein-protein interfaces.
  Acta Crystallogr D Biol Crystallogr, 63, 50-57.  
17567746 V.De Filippis, A.Draghi, R.Frasson, C.Grandi, V.Musi, A.Fontana, and A.Pastore (2007).
o-Nitrotyrosine and p-iodophenylalanine as spectroscopic probes for structural characterization of SH3 complexes.
  Protein Sci, 16, 1257-1265.  
16891373 H.X.Zhou (2006).
Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains.
  Biophys J, 91, 3170-3181.  
16498413 J.S.Woo, J.H.Imm, C.K.Min, K.J.Kim, S.S.Cha, and B.H.Oh (2006).
Structural and functional insights into the B30.2/SPRY domain.
  EMBO J, 25, 1353-1363.
PDB code: 2fnj
16766517 K.Ma, J.G.Forbes, G.Gutierrez-Cruz, and K.Wang (2006).
Titin as a giant scaffold for integrating stress and Src homology domain 3-mediated signaling pathways: the clustering of novel overlap ligand motifs in the elastic PEVK segment.
  J Biol Chem, 281, 27539-27556.  
16326715 K.Ogura, I.Nobuhisa, S.Yuzawa, R.Takeya, S.Torikai, K.Saikawa, H.Sumimoto, and F.Inagaki (2006).
NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide.
  J Biol Chem, 281, 3660-3668.
PDB code: 1wlp
16718600 M.L.Cartron, S.Maddocks, P.Gillingham, C.J.Craven, and S.C.Andrews (2006).
Feo--transport of ferrous iron into bacteria.
  Biometals, 19, 143-157.  
17132106 R.Stoll, S.Lodermeyer, and A.K.Bosserhoff (2006).
Detailed analysis of MIA protein by mutagenesis.
  Biol Chem, 387, 1601-1606.  
16600966 V.Musi, B.Birdsall, G.Fernandez-Ballester, R.Guerrini, S.Salvatori, L.Serrano, and A.Pastore (2006).
New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.
  Protein Sci, 15, 795-807.
PDB code: 2btt
16857672 X.Li, Y.Chen, Y.Liu, J.Gao, F.Gao, M.Bartlam, J.Y.Wu, and Z.Rao (2006).
Structural basis of Robo proline-rich motif recognition by the srGAP1 Src homology 3 domain in the Slit-Robo signaling pathway.
  J Biol Chem, 281, 28430-28437.
PDB code: 2gnc
15657040 C.Massenet, S.Chenavas, C.Cohen-Addad, M.C.Dagher, G.Brandolin, E.Pebay-Peyroula, and F.Fieschi (2005).
Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains.
  J Biol Chem, 280, 13752-13761.
PDB codes: 1w6x 1w70
16305332 G.U.Gangenahalli, V.K.Singh, Y.K.Verma, P.Gupta, R.K.Sharma, R.Chandra, S.Gulati, and P.M.Luthra (2005).
Three-dimensional structure prediction of the interaction of CD34 with the SH3 domain of Crk-L.
  Stem Cells Dev, 14, 470-477.  
15880548 L.J.Ball, R.Kühne, J.Schneider-Mergener, and H.Oschkinat (2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
  Angew Chem Int Ed Engl, 44, 2852-2869.  
15735341 P.Müller, M.R.Sawaya, I.Pashkov, S.Chan, C.Nguyen, Y.Wu, L.J.Perry, and D.Eisenberg (2005).
The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
  Acta Crystallogr D Biol Crystallogr, 61, 309-315.
PDB code: 1rii
14747998 B.Japelj, J.P.Waltho, and R.Jerala (2004).
Comparison of backbone dynamics of monomeric and domain-swapped stefin A.
  Proteins, 54, 500-512.  
15526038 H.Dvir, M.Harel, S.Bon, W.Q.Liu, M.Vidal, C.Garbay, J.L.Sussman, J.Massoulié, and I.Silman (2004).
The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.
  EMBO J, 23, 4394-4405.
PDB code: 1vzj
15200958 J.A.Marles, S.Dahesh, J.Haynes, B.J.Andrews, and A.R.Davidson (2004).
Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast.
  Mol Cell, 14, 813-823.  
12829691 A.V.Kurakin, S.Wu, and D.E.Bredesen (2003).
Atypical recognition consensus of CIN85/SETA/Ruk SH3 domains revealed by target-assisted iterative screening.
  J Biol Chem, 278, 34102-34109.  
12654250 O.Hantschel, B.Nagar, S.Guettler, J.Kretzschmar, K.Dorey, J.Kuriyan, and G.Superti-Furga (2003).
A myristoyl/phosphotyrosine switch regulates c-Abl.
  Cell, 112, 845-857.  
12482754 O.Olsen, and D.S.Bredt (2003).
Functional analysis of the nucleotide binding domain of membrane-associated guanylate kinases.
  J Biol Chem, 278, 6873-6878.  
12767128 S.L.Lam, and V.L.Hsu (2003).
NMR identification of left-handed polyproline type II helices.
  Biopolymers, 69, 270-281.  
14661268 W.D.Schubert, and D.W.Heinz (2003).
Structural aspects of adhesion to and invasion of host cells by the human pathogen Listeria monocytogenes.
  Chembiochem, 4, 1285-1291.  
12426371 C.Freund, R.Kühne, H.Yang, S.Park, E.L.Reinherz, and G.Wagner (2002).
Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules.
  EMBO J, 21, 5985-5995.
PDB code: 1l2z
11832214 H.Pluk, K.Dorey, and G.Superti-Furga (2002).
Autoinhibition of c-Abl.
  Cell, 108, 247-259.  
12079283 J.Xie, T.Cai, H.Zhang, M.S.Lan, and A.L.Notkins (2002).
The zinc-finger transcription factor INSM1 is expressed during embryo development and interacts with the Cbl-associated protein.
  Genomics, 80, 54-61.  
12191607 K.Parang, and P.A.Cole (2002).
Designing bisubstrate analog inhibitors for protein kinases.
  Pharmacol Ther, 93, 145-157.  
12384576 L.W.Donaldson, G.Gish, T.Pawson, L.E.Kay, and J.D.Forman-Kay (2002).
Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.
  Proc Natl Acad Sci U S A, 99, 14053-14058.
PDB code: 1ju5
12411480 M.Marino, M.Banerjee, R.Jonquières, P.Cossart, and P.Ghosh (2002).
GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.
  EMBO J, 21, 5623-5634.
PDB code: 1m9s
11723125 M.McLaughlin, R.Hale, D.Ellston, S.Gaudet, R.A.Lue, and A.Viel (2002).
The distribution and function of alternatively spliced insertions in hDlg.
  J Biol Chem, 277, 6406-6412.  
12441379 S.M.Larson, J.L.England, J.R.Desjarlais, and V.S.Pande (2002).
Thoroughly sampling sequence space: large-scale protein design of structural ensembles.
  Protein Sci, 11, 2804-2813.  
11929862 S.Panni, L.Dente, and G.Cesareni (2002).
In vitro evolution of recognition specificity mediated by SH3 domains reveals target recognition rules.
  J Biol Chem, 277, 21666-21674.  
11901150 T.Rose, and E.Di Cera (2002).
Three-dimensional modeling of thrombin-fibrinogen interaction.
  J Biol Chem, 277, 18875-18880.  
12370316 X.Li, and M.X.Guan (2002).
A human mitochondrial GTP binding protein related to tRNA modification may modulate phenotypic expression of the deafness-associated mitochondrial 12S rRNA mutation.
  Mol Cell Biol, 22, 7701-7711.  
12021428 Y.Liu, and D.Eisenberg (2002).
3D domain swapping: as domains continue to swap.
  Protein Sci, 11, 1285-1299.  
11779504 A.W.McGee, S.R.Dakoji, O.Olsen, D.S.Bredt, W.A.Lim, and K.E.Prehoda (2001).
Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.
  Mol Cell, 8, 1291-1301.
PDB code: 1kjw
11551507 C.L.Kielkopf, N.A.Rodionova, M.R.Green, and S.K.Burley (2001).
A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.
  Cell, 106, 595-605.
PDB code: 1jmt
11406576 M.Nishida, K.Nagata, Y.Hachimori, M.Horiuchi, K.Ogura, V.Mandiyan, J.Schlessinger, and F.Inagaki (2001).
Novel recognition mode between Vav and Grb2 SH3 domains.
  EMBO J, 20, 2995-3007.
PDB codes: 1gcp 1gcq
11141062 N.Okishio, T.Tanaka, R.Fukuda, and M.Nagai (2001).
Role of the conserved acidic residue Asp21 in the structure of phosphatidylinositol 3-kinase Src homology 3 domain: circular dichroism and nuclear magnetic resonance studies.
  Biochemistry, 40, 119-129.  
11157741 R.Stoll, C.Renner, M.Zweckstetter, M.Brüggert, D.Ambrosius, S.Palme, R.A.Engh, M.Golob, I.Breibach, R.Buettner, W.Voelter, T.A.Holak, and A.K.Bosserhoff (2001).
The extracellular human melanoma inhibitory activity (MIA) protein adopts an SH3 domain-like fold.
  EMBO J, 20, 340-349.
PDB code: 1hjd
10660573 A.J.Urquhart, D.Kennedy, S.J.Gould, and D.I.Crane (2000).
Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p.
  J Biol Chem, 275, 4127-4136.  
10873829 D.J.Owen, and J.P.Luzio (2000).
Structural insights into clathrin-mediated endocytosis.
  Curr Opin Cell Biol, 12, 467-474.  
10856234 H.Kang, C.Freund, J.S.Duke-Cohan, A.Musacchio, G.Wagner, and C.E.Rudd (2000).
SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55.
  EMBO J, 19, 2889-2899.  
10798399 J.Beneken, J.C.Tu, B.Xiao, M.Nuriya, J.P.Yuan, P.F.Worley, and D.J.Leahy (2000).
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition.
  Neuron, 26, 143-154.
PDB codes: 1ddv 1ddw
10919999 J.Kolafa, J.W.Perram, and R.P.Bywater (2000).
Essential motions and energetic contributions of individual residues in a peptide bound to an SH3 domain.
  Biophys J, 79, 646-655.  
10861385 N.Okishio, M.Nagai, R.Fukuda, S.Nagatomo, and T.Kitagawa (2000).
Interactions of phosphatidylinositol 3-kinase Src homology 3 domain with its ligand peptide studied by absorption, circular dichroism, and UV resonance raman spectroscopies.
  Biopolymers, 57, 208-217.  
10508163 A.M.Mongioví, P.R.Romano, S.Panni, M.Mendoza, W.T.Wong, A.Musacchio, G.Cesareni, and P.P.Di Fiore (1999).
A novel peptide-SH3 interaction.
  EMBO J, 18, 5300-5309.  
  10490629 A.W.Gross, X.Zhang, and R.Ren (1999).
Bcr-Abl with an SH3 deletion retains the ability To induce a myeloproliferative disease in mice, yet c-Abl activated by an SH3 deletion induces only lymphoid malignancy.
  Mol Cell Biol, 19, 6918-6928.  
10364172 A.W.McGee, and D.S.Bredt (1999).
Identification of an intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.
  J Biol Chem, 274, 17431-17436.  
10542231 G.Cestra, L.Castagnoli, L.Dente, O.Minenkova, A.Petrelli, N.Migone, U.Hoffmüller, J.Schneider-Mergener, and G.Cesareni (1999).
The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity.
  J Biol Chem, 274, 32001-32007.  
9988764 M.F.Denny, H.C.Kaufman, A.C.Chan, and D.B.Straus (1999).
The lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling.
  J Biol Chem, 274, 5146-5152.  
  10396139 M.Gautel, A.Mues, and P.Young (1999).
Control of sarcomeric assembly: the flow of information on titin.
  Rev Physiol Biochem Pharmacol, 138, 97.  
10090735 Q.Xu, J.Zheng, R.Xu, G.Barany, and D.Cowburn (1999).
Flexibility of interdomain contacts revealed by topological isomers of bivalent consolidated ligands to the dual Src homology domain SH(32) of abelson.
  Biochemistry, 38, 3491-3497.  
10441568 Y.Liu, J.Björkman, A.Urquhart, R.J.Wanders, D.I.Crane, and S.J.Gould (1999).
PEX13 is mutated in complementation group 13 of the peroxisome-biogenesis disorders.
  Am J Hum Genet, 65, 621-634.  
9736607 D.J.Owen, P.Wigge, Y.Vallis, J.D.Moore, P.R.Evans, and H.T.McMahon (1998).
Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation.
  EMBO J, 17, 5273-5285.
PDB code: 1bb9
9417118 J.W.Thomas, B.Ellis, R.J.Boerner, W.B.Knight, G.C.White, and M.D.Schaller (1998).
SH2- and SH3-mediated interactions between focal adhesion kinase and Src.
  J Biol Chem, 273, 577-583.  
  9573250 R.A.Lutzke, and R.H.Plasterk (1998).
Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: critical residues for protein oligomerization and DNA binding.
  J Virol, 72, 4841-4848.  
9629920 R.K.Rasmussen, H.Ji, J.S.Eddes, R.L.Moritz, G.E.Reid, R.J.Simpson, and D.S.Dorow (1998).
Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins.
  Electrophoresis, 19, 809-817.  
9811845 R.Sánchez, and A.Sali (1998).
Large-scale protein structure modeling of the Saccharomyces cerevisiae genome.
  Proc Natl Acad Sci U S A, 95, 13597-13602.  
9778343 S.Arold, R.O'Brien, P.Franken, M.P.Strub, F.Hoh, C.Dumas, and J.E.Ladbury (1998).
RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef.
  Biochemistry, 37, 14683-14691.
PDB code: 1bu1
9593201 S.Knapp, P.T.Mattson, P.Christova, K.D.Berndt, A.Karshikoff, M.Vihinen, C.I.Smith, and R.Ladenstein (1998).
Thermal unfolding of small proteins with SH3 domain folding pattern.
  Proteins, 31, 309-319.  
9566119 D.C.Dalgarno, M.C.Botfield, and R.J.Rickles (1997).
SH3 domains and drug design: ligands, structure, and biological function.
  Biopolymers, 43, 383-400.  
  9121467 I.de Mendez, N.Homayounpour, and T.L.Leto (1997).
Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation.
  Mol Cell Biol, 17, 2177-2185.  
9006901 J.D.Frantz, S.Giorgetti-Peraldi, E.A.Ottinger, and S.E.Shoelson (1997).
Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains.
  J Biol Chem, 272, 2659-2667.  
9241420 J.Kuriyan, and D.Cowburn (1997).
Modular peptide recognition domains in eukaryotic signaling.
  Annu Rev Biophys Biomol Struct, 26, 259-288.  
9287337 J.Meriläinen, V.P.Lehto, and V.M.Wasenius (1997).
FAP52, a novel, SH3 domain-containing focal adhesion protein.
  J Biol Chem, 272, 23278-23284.  
9351809 S.Arold, P.Franken, M.P.Strub, F.Hoh, S.Benichou, R.Benarous, and C.Dumas (1997).
The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
  Structure, 5, 1361-1372.
PDB codes: 1avv 1avz
8962058 A.Musacchio, L.C.Cantley, and S.C.Harrison (1996).
Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit.
  Proc Natl Acad Sci U S A, 93, 14373-14378.
PDB code: 1pbw
8805554 C.J.Morton, D.J.Pugh, E.L.Brown, J.D.Kahmann, D.A.Renzoni, and I.D.Campbell (1996).
Solution structure and peptide binding of the SH3 domain from human Fyn.
  Structure, 4, 705-714.
PDB codes: 1nyf 1nyg
8939757 C.S.Wright, and G.Hester (1996).
The 2.0 A structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes.
  Structure, 4, 1339-1352.
PDB code: 1jpc
8570618 C.Tribioli, S.Droetto, S.Bione, G.Cesareni, M.R.Torrisi, L.V.Lotti, L.Lanfrancone, D.Toniolo, and P.Pelicci (1996).
An X chromosome-linked gene encoding a protein with characteristics of a rhoGAP predominantly expressed in hematopoietic cells.
  Proc Natl Acad Sci U S A, 93, 695-699.  
8961927 D.A.Renzoni, D.J.Pugh, G.Siligardi, P.Das, C.J.Morton, C.Rossi, M.D.Waterfield, I.D.Campbell, and J.E.Ladbury (1996).
Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
  Biochemistry, 35, 15646-15653.
PDB codes: 1a0n 1azg
8789085 D.M.van Aalten, A.Amadei, R.Bywater, J.B.Findlay, H.J.Berendsen, C.Sander, and P.F.Stouten (1996).
A comparison of structural and dynamic properties of different simulation methods applied to SH3.
  Biophys J, 70, 684-692.  
8805596 H.J.Nam, W.G.Haser, T.M.Roberts, and C.A.Frederick (1996).
Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism.
  Structure, 4, 1105-1114.
PDB code: 2abl
8906616 M.C.Weiler, J.L.Smith, and J.N.Masters (1996).
CR16, a novel proline-rich protein expressed in rat brain neurons, binds to SH3 domains and is a MAP kinase substrate.
  J Mol Neurosci, 7, 203-215.  
  8649366 M.E.Nickas, and M.P.Yaffe (1996).
BRO1, a novel gene that interacts with components of the Pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae.
  Mol Cell Biol, 16, 2585-2593.  
8662907 M.Matsuda, S.Ota, R.Tanimura, H.Nakamura, K.Matuoka, T.Takenawa, K.Nagashima, and T.Kurata (1996).
Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins.
  J Biol Chem, 271, 14468-14472.  
8718852 M.T.Pisabarro, and L.Serrano (1996).
Rational design of specific high-affinity peptide ligands for the Abl-SH3 domain.
  Biochemistry, 35, 10634-10640.  
8824280 P.M.Finan, C.J.Soames, L.Wilson, D.L.Nelson, D.M.Stewart, O.Truong, J.J.Hsuan, and S.Kellie (1996).
Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains.
  J Biol Chem, 271, 26291-26295.  
8807900 S.Feng, T.M.Kapoor, F.Shirai, A.P.Combs, and S.L.Schreiber (1996).
Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis.
  Chem Biol, 3, 661-670.
PDB codes: 1nlo 1nlp
8805558 W.A.Lim (1996).
Reading between the lines: SH3 recognition of an intact protein.
  Structure, 4, 657-659.  
8798569 X.Zhu, N.S.Lamango, and I.Lindberg (1996).
Involvement of a polyproline helix-like structure in the interaction of 7B2 with prohormone convertase 2.
  J Biol Chem, 271, 23582-23587.  
7542990 B.J.Mayer, and M.J.Eck (1995).
SH3 domains. Minding your p's and q's.
  Curr Biol, 5, 364-367.  
  7774577 B.S.Knudsen, J.Zheng, S.M.Feller, J.P.Mayer, S.K.Burrell, D.Cowburn, and H.Hanafusa (1995).
Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins.
  EMBO J, 14, 2191-2198.  
  7588629 C.H.Lee, B.Leung, M.A.Lemmon, J.Zheng, D.Cowburn, J.Kuriyan, and K.Saksela (1995).
A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein.
  EMBO J, 14, 5006-5015.  
7797522 C.Schumacher, B.S.Knudsen, T.Ohuchi, P.P.Di Fiore, R.H.Glassman, and H.Hanafusa (1995).
The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R.
  J Biol Chem, 270, 15341-15347.  
7592905 D.Cowburn, J.Zheng, Q.Xu, and G.Barany (1995).
Enhanced affinities and specificities of consolidated ligands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine kinase.
  J Biol Chem, 270, 26738-26741.  
7834743 G.B.Cohen, R.Ren, and D.Baltimore (1995).
Modular binding domains in signal transduction proteins.
  Cell, 80, 237-248.  
9383403 J.A.Simon, and S.L.Schreiber (1995).
Grb2 SH3 binding to peptides from Sos: evaluation of a general model for SH3-ligand interactions.
  Chem Biol, 2, 53-60.  
7536925 K.Alexandropoulos, G.Cheng, and D.Baltimore (1995).
Proline-rich sequences that bind to Src homology 3 domains with individual specificities.
  Proc Natl Acad Sci U S A, 92, 3110-3114.  
  7744002 M.Gautel, O.Zuffardi, A.Freiburg, and S.Labeit (1995).
Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?
  EMBO J, 14, 1952-1960.  
7773739 R.L.Stanfield, and I.A.Wilson (1995).
Protein-peptide interactions.
  Curr Opin Struct Biol, 5, 103-113.  
8618911 S.Feng, C.Kasahara, R.J.Rickles, and S.L.Schreiber (1995).
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.
  Proc Natl Acad Sci U S A, 92, 12408-12415.
PDB codes: 1qwe 1qwf
7629138 S.S.Yang, L.Van Aelst, and D.Bar-Sagi (1995).
Differential interactions of human Sos1 and Sos2 with Grb2.
  J Biol Chem, 270, 18212-18215.  
  7534229 T.Erpel, G.Superti-Furga, and S.A.Courtneidge (1995).
Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions.
  EMBO J, 14, 963-975.  
7735837 X.Wu, B.Knudsen, S.M.Feller, J.Zheng, A.Sali, D.Cowburn, H.Hanafusa, and J.Kuriyan (1995).
Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk.
  Structure, 3, 215-226.
PDB codes: 1cka 1ckb
8590002 Y.Q.Gosser, J.Zheng, M.Overduin, B.J.Mayer, and D.Cowburn (1995).
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
  Structure, 3, 1075-1086.
PDB code: 1awo
  7565714 Z.Weng, R.J.Rickles, S.Feng, S.Richard, A.S.Shaw, S.L.Schreiber, and J.S.Brugge (1995).
Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions.
  Mol Cell Biol, 15, 5627-5634.  
7855886 S.M.Feller, R.Ren, H.Hanafusa, and D.Baltimore (1994).
SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl.
  Trends Biochem Sci, 19, 453-458.  
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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