1AOT
NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, MINIMIZED AVERAGE STRUCTURE
1AOT の概要
| エントリーDOI | 10.2210/pdb1aot/pdb |
| 関連するPDBエントリー | 1AOU |
| 分子名称 | FYN PROTEIN-TYROSINE KINASE, PHOSPHOTYROSYL PEPTIDE (2 entities in total) |
| 機能のキーワード | sh2 domain, signal transduction, peptide complex, complex (proto-oncogene-early protein), complex (proto-oncogene-early protein) complex, complex (proto-oncogene/early protein) |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cell membrane: P06241 Host membrane; Single-pass membrane protein (Potential): P03079 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 13773.33 |
| 構造登録者 | Mulhern, T.D.,Shaw, G.L.,Morton, C.J.,Day, A.J.,Campbell, I.D. (登録日: 1997-07-10, 公開日: 1998-01-14, 最終更新日: 2024-10-23) |
| 主引用文献 | Mulhern, T.D.,Shaw, G.L.,Morton, C.J.,Day, A.J.,Campbell, I.D. The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. Structure, 5:1313-1323, 1997 Cited by PubMed Abstract: SH2 domains are found in a variety of signal transduction proteins; they bind phosphotyrosine-containing sequences, allowing them to both recognize target molecules and regulate intramolecular kinase activity. Fyn is a member of the Src family of tyrosine kinases that are involved in signal transduction by association with a number of membrane receptors. The kinase activity of these signalling proteins is modulated by switching the binding mode of their SH2 and SH3 domains from intramolecular to intermolecular. The molecular basis of the signalling roles observed for different Src family members is still not well understood; although structures have been determined for the SH2 domains of other Src family molecules, this is the first structure of the Fyn SH2 domain. PubMed: 9351806DOI: 10.1016/S0969-2126(97)00283-9 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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