1AYC

CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE

Summary for 1AYC

• Entry DOI: 10.2210/pdb1ayc/pdb
• Descriptor: PROTEIN-TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN), PEPTIDE PDGFR-740 (3 entities in total)
• Functional Keywords: hydrolase(sh2 domain)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm: P35235; Membrane; Single-pass type I membrane protein: P05622
• Total number of polymer chains: 2
• Total formula weight: 12757.20

Authors

Lee, C.-H.,Kuriyan, J. (deposition date: 1994-05-15, release date: 1994-08-31, Last modification date: 2024-10-30)

Primary citation

Lee, C.H.,Kominos, D.,Jacques, S.,Margolis, B.,Schlessinger, J.,Shoelson, S.E.,Kuriyan, J.
Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.
Structure, 2:423-438, 1994

PubMed Abstract: 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.

PubMed: 7521735
DOI: 10.1016/S0969-2126(00)00044-7

Experimental method

X-RAY DIFFRACTION (2.3 Å)