1AYC
CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE
1AYC の概要
エントリーDOI | 10.2210/pdb1ayc/pdb |
分子名称 | PROTEIN-TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN), PEPTIDE PDGFR-740 (3 entities in total) |
機能のキーワード | hydrolase(sh2 domain) |
由来する生物種 | Mus musculus (house mouse) 詳細 |
細胞内の位置 | Cytoplasm: P35235 Membrane; Single-pass type I membrane protein: P05622 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 12757.20 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 7521735DOI: 10.1016/S0969-2126(00)00044-7 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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