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1CSY

SYK TYROSINE KINASE C-TERMINAL SH2 DOMAIN COMPLEXED WITH A PHOSPHOPEPTIDEFROM THE GAMMA CHAIN OF THE HIGH AFFINITY IMMUNOGLOBIN G RECEPTOR, NMR

1CSY の概要
エントリーDOI10.2210/pdb1csy/pdb
分子名称SYK PROTEIN TYROSINE KINASE, ACETYL-THR-PTR-GLU-THR-LEU-NH2 (2 entities in total)
機能のキーワードprotein-tyrosine kinase sh2 domain, complex (phosphotransferase-peptide), complex (phosphotransferase-peptide) complex, complex (phosphotransferase/peptide)
由来する生物種Homo sapiens (human)
詳細
タンパク質・核酸の鎖数2
化学式量合計13464.36
構造登録者
主引用文献Narula, S.S.,Yuan, R.W.,Adams, S.E.,Green, O.M.,Green, J.,Philips, T.B.,Zydowsky, L.D.,Botfield, M.C.,Hatada, M.,Laird, E.R.,Zoller, M.J.,Karas, J.L.,Dalgarno, D.C.
Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide.
Structure, 3:1061-1073, 1995
Cited by
PubMed Abstract: Recruitment of the intracellular tyrosine kinase Syk to activated immune-response receptors is a critical early step in intracellular signaling. In mast cells, Syk specifically associates with doubly phosphorylated immunoreceptor tyrosine-based activation motifs (ITAMs) that are found within the IgE receptor. The mechanism by which Syk recognizes these motifs is not fully understood. Both Syk SH2 (Src homology 2) domains are required for high-affinity binding to these motifs, but the C-terminal SH2 domain (Syk-C) can function independently and can bind, in isolation, to the tyrosine-phosphorylated IgE receptor in vitro. In order to improve understanding of the cellular function of Syk, we have determined the solution structure of Syk-C complexed with a phosphotyrosine peptide derived from the gamma subunit of the IgE receptor.
PubMed: 8590001
DOI: 10.1016/S0969-2126(01)00242-8
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1csy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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