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1AWO

THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2 IN THE SH(32) CONSTRUCT, 20 STRUCTURES

1AWO の概要
エントリーDOI10.2210/pdb1awo/pdb
分子名称ABL TYROSINE KINASE (1 entity in total)
機能のキーワードkinase, sh3 domain, transferase, phosphotransferase, proto-oncogene, multiple domain, leukemia
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519
タンパク質・核酸の鎖数1
化学式量合計6637.30
構造登録者
Cowburn, D. (登録日: 1997-10-03, 公開日: 1998-01-28, 最終更新日: 2024-05-22)
主引用文献Gosser, Y.Q.,Zheng, J.,Overduin, M.,Mayer, B.J.,Cowburn, D.
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
Structure, 3:1075-1086, 1995
Cited by
PubMed Abstract: The Src homology domains, SH3 and SH2, of Abl protein tyrosine kinase regulate enzymatic activity in vivo. Abl SH3 suppresses kinase activity, whereas Abl SH2 is required for the transforming activity of the activated form of Abl. We expect that the solution structures of Abl SH3, Abl SH2 and Abl SH(32) (a dual domain comprising SH3 and SH2 subdomains) will contribute to a structural basis for understanding the mechanism of the Abl 'regulatory apparatus'.
PubMed: 8590002
DOI: 10.1016/S0969-2126(01)00243-X
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 1awo
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2026-04-29に公開中

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