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DOI | 10.2210/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 | |
| 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: 8590002DOI: 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 |
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