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PDBsum entry 1ayb

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Hydrolase(sh2 domain) PDB id
1ayb
Jmol
Contents
Protein chain
100 a.a. *
Ligands
GLY-GLU-PTR-VAL-
ASN-ILE-GLU-PHE
* Residue conservation analysis
PDB id:
1ayb
Name: Hydrolase(sh2 domain)
Title: Crystal structures of peptide complexes of the amino- terminal sh2 domain of the syp tyrosine phosphatase
Structure: Protein-tyrosine phosphatase syp (n-terminal sh2 domain). Chain: a. Engineered: yes. Peptide irs-1-895. Chain: p. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090
Biol. unit: Tetramer (from PQS)
Resolution:
3.00Å     R-factor:   0.164    
Authors: C.-H.Lee,J.Kuriyan
Key ref:
C.H.Lee et al. (1994). Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure, 2, 423-438. PubMed id: 7521735 DOI: 10.1016/S0969-2126(00)00044-7
Date:
15-May-94     Release date:   31-Aug-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P35235  (PTN11_MOUSE) -  Tyrosine-protein phosphatase non-receptor type 11
Seq:
Struc:
 
Seq:
Struc:
597 a.a.
100 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
Bound ligand (Het Group name = PTR)
matches with 76.00% similarity
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/S0969-2126(00)00044-7 Structure 2:423-438 (1994)
PubMed id: 7521735  
 
 
Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.
C.H.Lee, D.Kominos, S.Jacques, B.Margolis, J.Schlessinger, S.E.Shoelson, J.Kuriyan.
 
  ABSTRACT  
 
BACKGROUND: Src homology 2 (SH2) domains bind to phosphotyrosine residues in a sequence-specific manner, and thereby couple tyrosine phosphorylation to changes in the localization or catalytic activity of signal transducing molecules. Current understanding of SH2 specificity is based on the structures of SH2-peptide complexes of the closely-related Src and Lck tyrosine kinases. The tyrosine phosphatase Syp contains two SH2 domains that are relatively divergent from those of the tyrosine kinases, with distinct target specificities, and is thus well suited for structural studies aimed at extending our understanding of SH2 specificity. RESULTS: Crystal structures of the amino-terminal SH2 domain of Syp in separate complexes with two high-affinity peptides, in complex with a non-specific peptide and in the uncomplexed form have been determined at between 2 A and 3 A resolution. The structure of the SH2 domain and the mode of high-affinity peptide binding is essentially similar to that seen in the Src and Lck structures. However, the binding interface is more extensive in Syp. CONCLUSIONS: Most SH2 targets have hydrophobic residues at the third position following the phosphotyrosine, and the Syp structure confirms that the peptide is anchored to the SH2 surface by this residue and by the phosphotyrosine. In addition, the Syp structure has revealed that sequence specificity can extend across the five residues following the phosphotyrosine, and has shown how the SH2 domain's surface topography can be altered with resulting changes in specificity, while conserving the structure of the central core of the domain.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Comparison of the Syp and Src SH2 domains. The polypeptide backbones of the Syp and Src SH2 domains are shown as red and white tubes, respectively. The YEEI peptide (Src) is shown in yellow and the IRS1-895 and PDGFR-1009 peptides (Syp) are shown in orange and blue, respectively. The view is approximately perpendicular to the peptide-binding surface. The two structures were first superimposed with the program O [44] and displayed using Insight (Biosym Technologies). Figure 4. Comparison of the Syp and Src SH2 domains. The polypeptide backbones of the Syp and Src SH2 domains are shown as red and white tubes, respectively. The YEEI peptide (Src) is shown in yellow and the IRS1-895 and PDGFR-1009 peptides (Syp) are shown in orange and blue, respectively. The view is approximately perpendicular to the peptide-binding surface. The two structures were first superimposed with the program O [[3]44] and displayed using Insight (Biosym Technologies).
 
  The above figure is reprinted by permission from Cell Press: Structure (1994, 2, 423-438) copyright 1994.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21419780 D.Close, S.J.Johnson, M.A.Sdano, S.M.McDonald, H.Robinson, T.Formosa, and C.P.Hill (2011).
Crystal Structures of the S. cerevisiae Spt6 Core and C-Terminal Tandem SH2 Domain.
  J Mol Biol, 408, 697-713.
PDB codes: 3psf 3psi 3psj 3psk
21365683 E.Darian, O.Guvench, B.Yu, C.K.Qu, and A.D.Mackerell (2011).
Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase.
  Proteins, 79, 1573-1588.  
19768778 K.Teichmann, T.Kühl, I.Könnig, K.Wieligmann, M.Zacharias, and D.Imhof (2010).
Modulation of SHP-1 phosphatase activity by monovalent and bivalent SH2 phosphopeptide ligands.
  Biopolymers, 93, 102-112.  
19771558 M.Guttman, G.N.Betts, H.Barnes, M.Ghassemian, P.van der Geer, and E.A.Komives (2009).
Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1.
  Proteomics, 9, 5016-5028.  
18721752 A.Kaushansky, A.Gordus, B.A.Budnik, W.S.Lane, J.Rush, and G.MacBeath (2008).
System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties.
  Chem Biol, 15, 808-817.  
18493663 A.Kaushansky, A.Gordus, B.Chang, J.Rush, and G.MacBeath (2008).
A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R.
  Mol Biosyst, 4, 643-653.  
18260110 I.Lappalainen, J.Thusberg, B.Shen, and M.Vihinen (2008).
Genome wide analysis of pathogenic SH2 domain mutations.
  Proteins, 72, 779-792.  
18372317 S.Martinelli, P.Torreri, M.Tinti, L.Stella, G.Bocchinfuso, E.Flex, A.Grottesi, M.Ceccarini, A.Palleschi, G.Cesareni, L.Castagnoli, T.C.Petrucci, B.D.Gelb, and M.Tartaglia (2008).
Diverse driving forces underlie the invariant occurrence of the T42A, E139D, I282V and T468M SHP2 amino acid substitutions causing Noonan and LEOPARD syndromes.
  Hum Mol Genet, 17, 2018-2029.  
17997974 A.N.Bullock, M.C.Rodriguez, J.E.Debreczeni, Z.Songyang, and S.Knapp (2007).
Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation.
  Structure, 15, 1493-1504.
PDB code: 2izv
17177198 G.Bocchinfuso, L.Stella, S.Martinelli, E.Flex, C.Carta, F.Pantaleoni, B.Pispisa, M.Venanzi, M.Tartaglia, and A.Palleschi (2007).
Structural and functional effects of disease-causing amino acid substitutions affecting residues Ala72 and Glu76 of the protein tyrosine phosphatase SHP-2.
  Proteins, 66, 963-974.  
17378938 O.Guvench, C.K.Qu, and A.D.MacKerell (2007).
Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft.
  BMC Struct Biol, 7, 14.  
16702225 D.Imhof, A.S.Wavreille, A.May, M.Zacharias, S.Tridandapani, and D.Pei (2006).
Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains. Critical roles of residues beyond the pY+3 position.
  J Biol Chem, 281, 20271-20282.  
16905102 E.Bergamin, J.Wu, and S.R.Hubbard (2006).
Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3.
  Structure, 14, 1285-1292.
PDB code: 2hmh
16902940 K.Hampel, I.Kaufhold, M.Zacharias, F.D.Böhmer, and D.Imhof (2006).
Phosphopeptide ligands of the SHP-1 N-SH2 domain: effects on binding and stimulation of phosphatase activity.
  ChemMedChem, 1, 869-877.  
15959902 A.C.Roque, and C.R.Lowe (2005).
Lessons from nature: On the molecular recognition elements of the phosphoprotein binding-domains.
  Biotechnol Bioeng, 91, 546-555.  
15841400 C.J.Porter, M.C.Wilce, J.P.Mackay, P.Leedman, and J.A.Wilce (2005).
Grb7-SH2 domain dimerisation is affected by a single point mutation.
  Eur Biophys J, 34, 454-460.  
15987685 H.Keilhack, F.S.David, M.McGregor, L.C.Cantley, and B.G.Neel (2005).
Diverse biochemical properties of Shp2 mutants. Implications for disease phenotypes.
  J Biol Chem, 280, 30984-30993.  
16124853 M.Tartaglia, and B.D.Gelb (2005).
Noonan syndrome and related disorders: genetics and pathogenesis.
  Annu Rev Genomics Hum Genet, 6, 45-68.  
15769739 T.Avril, S.D.Freeman, H.Attrill, R.G.Clarke, and P.R.Crocker (2005).
Siglec-5 (CD170) can mediate inhibitory signaling in the absence of immunoreceptor tyrosine-based inhibitory motif phosphorylation.
  J Biol Chem, 280, 19843-19851.  
15521065 W.H.Lee, A.Raas-Rotschild, M.A.Miteva, G.Bolasco, A.Rein, D.Gillis, D.Vidaud, M.Vidaud, B.O.Villoutreix, and B.Parfait (2005).
Noonan syndrome type I with PTPN11 3 bp deletion: structure-function implications.
  Proteins, 58, 7.  
15384080 D.R.Bertola, A.C.Pereira, P.S.de Oliveira, C.A.Kim, and J.E.Krieger (2004).
Clinical variability in a Noonan syndrome family with a new PTPN11 gene mutation.
  Am J Med Genet A, 130, 378-383.  
12767128 S.L.Lam, and V.L.Hsu (2003).
NMR identification of left-handed polyproline type II helices.
  Biopolymers, 69, 270-281.  
12688310 S.M.Feller, G.Tuchscherer, and J.Voss (2003).
High affinity molecules disrupting GRB2 protein complexes as a therapeutic strategy for chronic myelogenous leukaemia.
  Leuk Lymphoma, 44, 411-427.  
12395395 B.Bochicchio, and A.M.Tamburro (2002).
Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions.
  Chirality, 14, 782-792.  
12119038 D.De Souza, L.J.Fabri, A.Nash, D.J.Hilton, N.A.Nicola, and M.Baca (2002).
SH2 domains from suppressor of cytokine signaling-3 and protein tyrosine phosphatase SHP-2 have similar binding specificities.
  Biochemistry, 41, 9229-9236.  
11994738 M.B.Yaffe (2002).
Phosphotyrosine-binding domains in signal transduction.
  Nat Rev Mol Cell Biol, 3, 177-186.  
12027890 M.Hörtner, U.Nielsch, L.M.Mayr, P.C.Heinrich, and S.Haan (2002).
A new high affinity binding site for suppressor of cytokine signaling-3 on the erythropoietin receptor.
  Eur J Biochem, 269, 2516-2526.  
11992261 M.Tartaglia, K.Kalidas, A.Shaw, X.Song, D.L.Musat, I.van der Burgt, H.G.Brunner, D.R.Bertola, A.Crosby, A.Ion, R.S.Kucherlapati, S.Jeffery, M.A.Patton, and B.D.Gelb (2002).
PTPN11 mutations in Noonan syndrome: molecular spectrum, genotype-phenotype correlation, and phenotypic heterogeneity.
  Am J Hum Genet, 70, 1555-1563.  
11746693 G.M.Verkhivker, D.Bouzida, D.K.Gehlhaar, P.A.Rejto, L.Schaffer, S.Arthurs, A.B.Colson, S.T.Freer, V.Larson, B.A.Luty, T.Marrone, and P.W.Rose (2001).
Hierarchy of simulation models in predicting molecular recognition mechanisms from the binding energy landscapes: structural analysis of the peptide complexes with SH2 domains.
  Proteins, 45, 456-470.  
11704759 M.Tartaglia, E.L.Mehler, R.Goldberg, G.Zampino, H.G.Brunner, H.Kremer, I.van der Burgt, A.H.Crosby, A.Ion, S.Jeffery, K.Kalidas, M.A.Patton, R.S.Kucherlapati, and B.D.Gelb (2001).
Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome.
  Nat Genet, 29, 465-468.  
11052678 K.D.Beebe, P.Wang, G.Arabaci, and D.Pei (2000).
Determination of the binding specificity of the SH2 domains of protein tyrosine phosphatase SHP-1 through the screening of a combinatorial phosphotyrosyl peptide library.
  Biochemistry, 39, 13251-13260.  
11063574 N.Schiering, E.Casale, P.Caccia, P.Giordano, and C.Battistini (2000).
Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex.
  Biochemistry, 39, 13376-13382.
PDB code: 1fyr
10829066 S.E.Nicholson, D.De Souza, L.J.Fabri, J.Corbin, T.A.Willson, J.G.Zhang, A.Silva, M.Asimakis, A.Farley, A.D.Nash, D.Metcalf, D.J.Hilton, N.A.Nicola, and M.Baca (2000).
Suppressor of cytokine signaling-3 preferentially binds to the SHP-2-binding site on the shared cytokine receptor subunit gp130.
  Proc Natl Acad Sci U S A, 97, 6493-6498.  
9551546 D.Barford, and B.G.Neel (1998).
Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2.
  Structure, 6, 249-254.  
9485424 G.Huyer, and C.Ramachandran (1998).
The specificity of the N-terminal SH2 domain of SHP-2 is modified by a single point mutation.
  Biochemistry, 37, 2741-2747.  
9612082 J.C.Williams, R.K.Wierenga, and M.Saraste (1998).
Insights into Src kinase functions: structural comparisons.
  Trends Biochem Sci, 23, 179-184.  
9636054 J.M.Bradshaw, R.A.Grucza, J.E.Ladbury, and G.Waksman (1998).
Probing the "two-pronged plug two-holed socket" model for the mechanism of binding of the Src SH2 domain to phosphotyrosyl peptides: a thermodynamic study.
  Biochemistry, 37, 9083-9090.  
9461082 L.E.Kay, D.R.Muhandiram, G.Wolf, S.E.Shoelson, and J.D.Forman-Kay (1998).
Correlation between binding and dynamics at SH2 domain interfaces.
  Nat Struct Biol, 5, 156-163.  
9665181 L.E.Kay (1998).
Protein dynamics from NMR.
  Nat Struct Biol, 5, 513-517.  
9838094 M.J.Bottomley, K.Salim, and G.Panayotou (1998).
Phospholipid-binding protein domains.
  Biochim Biophys Acta, 1436, 165-183.  
9491886 P.Hof, S.Pluskey, S.Dhe-Paganon, M.J.Eck, and S.E.Shoelson (1998).
Crystal structure of the tyrosine phosphatase SHP-2.
  Cell, 92, 441-450.
PDB code: 2shp
  9447970 T.Itoh, R.Liu, T.Yokota, K.I.Arai, and S.Watanabe (1998).
Definition of the role of tyrosine residues of the common beta subunit regulating multiple signaling pathways of granulocyte-macrophage colony-stimulating factor receptor.
  Mol Cell Biol, 18, 742-752.  
9817027 T.K.Sawyer (1998).
Src homology-2 domains: structure, mechanisms, and drug discovery.
  Biopolymers, 47, 243-261.  
  9300491 A.U.Singer, and J.D.Forman-Kay (1997).
pH titration studies of an SH2 domain-phosphopeptide complex: unusual histidine and phosphate pKa values.
  Protein Sci, 6, 1910-1919.  
9153411 B.Gay, P.Furet, C.García-Echeverría, J.Rahuel, P.Chène, H.Fretz, J.Schoepfer, and G.Caravatti (1997).
Dual specificity of Src homology 2 domains for phosphotyrosine peptide ligands.
  Biochemistry, 36, 5712-5718.  
9254595 C.McNemar, M.E.Snow, W.T.Windsor, A.Prongay, P.Mui, R.Zhang, J.Durkin, H.V.Le, and P.C.Weber (1997).
Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2.
  Biochemistry, 36, 10006-10014.  
9241420 J.Kuriyan, and D.Cowburn (1997).
Modular peptide recognition domains in eukaryotic signaling.
  Annu Rev Biophys Biomol Struct, 26, 259-288.  
9174343 P.S.Charifson, L.M.Shewchuk, W.Rocque, C.W.Hummel, S.R.Jordan, C.Mohr, G.J.Pacofsky, M.R.Peel, M.Rodriguez, D.D.Sternbach, and T.G.Consler (1997).
Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study.
  Biochemistry, 36, 6283-6293.
PDB codes: 1a07 1a08 1a09 1a1a 1a1b 1a1c 1a1e
9667855 S.E.Shoelson (1997).
SH2 and PTB domain interactions in tyrosine kinase signal transduction.
  Curr Opin Chem Biol, 1, 227-234.  
9351806 T.D.Mulhern, G.L.Shaw, C.J.Morton, A.J.Day, and I.D.Campbell (1997).
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
  Structure, 5, 1313-1323.
PDB codes: 1aot 1aou
9171349 T.M.Saxton, M.Henkemeyer, S.Gasca, R.Shen, D.J.Rossi, F.Shalaby, G.S.Feng, and T.Pawson (1997).
Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.
  EMBO J, 16, 2352-2364.  
9321393 Z.Zhang, C.H.Lee, V.Mandiyan, J.P.Borg, B.Margolis, J.Schlessinger, and J.Kuriyan (1997).
Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain.
  EMBO J, 16, 6141-6150.
PDB codes: 1aqc 1x11
  8670861 A.L.Breeze, B.V.Kara, D.G.Barratt, M.Anderson, J.C.Smith, R.W.Luke, J.R.Best, and S.A.Cartlidge (1996).
Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase.
  EMBO J, 15, 3579-3589.
PDB code: 1pic
8577729 D.Pei, J.Wang, and C.T.Walsh (1996).
Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1.
  Proc Natl Acad Sci U S A, 93, 1141-1145.  
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
8780508 J.E.Ladbury, M.Hensmann, G.Panayotou, and I.D.Campbell (1996).
Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: implications for regulation of tyrosine kinase activity.
  Biochemistry, 35, 11062-11069.  
8673601 J.Rahuel, B.Gay, D.Erdmann, A.Strauss, C.Garcia-Echeverría, P.Furet, G.Caravatti, H.Fretz, J.Schoepfer, and M.G.Grütter (1996).
Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode.
  Nat Struct Biol, 3, 586-589.
PDB code: 1tze
8794768 K.H.Thornton, W.T.Mueller, P.McConnell, G.Zhu, A.R.Saltiel, and V.Thanabal (1996).
Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain.
  Biochemistry, 35, 11852-11864.
PDB code: 1ghu
8555205 L.E.Kay, D.R.Muhandiram, N.A.Farrow, Y.Aubin, and J.D.Forman-Kay (1996).
Correlation between dynamics and high affinity binding in an SH2 domain interaction.
  Biochemistry, 35, 361-368.  
8672527 M.T.Brown, and J.A.Cooper (1996).
Regulation, substrates and functions of src.
  Biochim Biophys Acta, 1287, 121-149.  
8577769 P.van der Geer, S.Wiley, G.D.Gish, V.K.Lai, R.Stephens, M.F.White, D.Kaplan, and T.Pawson (1996).
Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites.
  Proc Natl Acad Sci U S A, 93, 963-968.  
8599763 R.T.Nolte, M.J.Eck, J.Schlessinger, S.E.Shoelson, and S.C.Harrison (1996).
Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes.
  Nat Struct Biol, 3, 364-374.
PDB codes: 2iug 2iuh 2iui
  8868476 S.Réty, K.Fütterer, R.A.Grucza, C.M.Munoz, W.A.Frazier, and G.Waksman (1996).
pH-Dependent self-association of the Src homology 2 (SH2) domain of the Src homologous and collagen-like (SHC) protein.
  Protein Sci, 5, 405-413.  
8952511 U.L.Günther, Y.Liu, D.Sanford, W.W.Bachovchin, and B.Schaffhausen (1996).
NMR analysis of interactions of a phosphatidylinositol 3'-kinase SH2 domain with phosphotyrosine peptides reveals interdependence of major binding sites.
  Biochemistry, 35, 15570-15581.  
8639560 W.J.Metzler, B.Leiting, K.Pryor, L.Mueller, and B.T.Farmer (1996).
The three-dimensional solution structure of the SH2 domain from p55blk kinase.
  Biochemistry, 35, 6201-6211.
PDB codes: 1blj 1blk
7542925 B.Schaffhausen (1995).
SH2 domain structure and function.
  Biochim Biophys Acta, 1242, 61-75.  
8846213 D.Barford, Z.Jia, and N.K.Tonks (1995).
Protein tyrosine phosphatases take off.
  Nat Struct Biol, 2, 1043-1053.  
7834743 G.B.Cohen, R.Ren, and D.Baltimore (1995).
Modular binding domains in signal transduction proteins.
  Cell, 80, 237-248.  
7540055 G.Siligardi, and A.F.Drake (1995).
The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides.
  Biopolymers, 37, 281-292.  
8564419 K.Ramalingam, S.R.Eaton, W.L.Cody, G.H.Lu, R.L.Panek, L.A.Waite, S.J.Decker, J.A.Keiser, and A.M.Doherty (1995).
Structure-activity studies of phosphorylated peptide inhibitors of the association of phosphatidylinositol 3-kinase with PDGF-beta receptor.
  Bioorg Med Chem, 3, 1263-1272.  
7773739 R.L.Stanfield, and I.A.Wilson (1995).
Protein-peptide interactions.
  Curr Opin Struct Biol, 5, 103-113.  
8590001 S.S.Narula, R.W.Yuan, S.E.Adams, O.M.Green, J.Green, T.B.Philips, L.D.Zydowsky, M.C.Botfield, M.Hatada, and E.R.Laird (1995).
Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide.
  Structure, 3, 1061-1073.
PDB codes: 1csy 1csz
7889566 U.Klingmüller, U.Lorenz, L.C.Cantley, B.G.Neel, and H.F.Lodish (1995).
Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals.
  Cell, 80, 729-738.  
8578591 Z.Songyang, and L.C.Cantley (1995).
Recognition and specificity in protein tyrosine kinase-mediated signalling.
  Trends Biochem Sci, 20, 470-475.  
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.