1FU5

NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM POLYOMAVIRUS MIDDLE T ANTIGEN

1FU5 の概要

• エントリーDOI: 10.2210/pdb1fu5/pdb
• 関連するPDBエントリー: 1FU6
• 分子名称: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT, DOUBLY PHOSPHORYLATED MIDDLE T ANTIGEN (2 entities in total)
• 機能のキーワード: protein-peptide complex, peptide binding protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Host membrane; Single-pass membrane protein (Potential): P03076
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14933.47

構造登録者

Weber, T.,Schaffhausen, B.,Liu, Y.,Guenther, U.L. (登録日: 2000-09-14, 公開日: 2001-02-21, 最終更新日: 2024-11-13)

主引用文献

Weber, T.,Schaffhausen, B.,Liu, Y.,Gunther, U.L.
NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.
Biochemistry, 39:15860-15869, 2000

PubMed Abstract: The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a higher affinity for a peptide with two phosphotyrosines than for the same peptide with only one. This unexpected result was not observed for the C-terminal SH2 from the same protein. NMR structural analysis has been used to understand the behavior of the N-SH2. The structure of the free SH2 domain has been compared to that of the SH2 complexed with a doubly phosphorylated peptide derived from polyomavirus middle T antigen (MT). The structure of the free SH2 domain shows some differences from previous NMR and X-ray structures. In the N-SH2 complexed with a doubly phosphorylated peptide, a second site for phosphotyrosine interaction has been identified. Further, line shapes of NMR signals showed that the SH2 protein-ligand complex is subject to temperature-dependent conformational mobility. Conformational mobility is also supported by the spectra of the ligand peptide. A binding model which accounts for these results is developed.

PubMed: 11123912
DOI: 10.1021/bi001474d

実験手法

SOLUTION NMR