2NWM

Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin

2NWM の概要

• エントリーDOI: 10.2210/pdb2nwm/pdb
• 分子名称: Vinexin (1 entity in total)
• 機能のキーワード: vinexin sh3 domain, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform Alpha: Cell junction (By similarity). Isoform Beta: Cell junction (By similarity): O60504
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7688.76

構造登録者

Zhang, J.,Yao, B.,Wu, J.,Shi, Y. (登録日: 2006-11-15, 公開日: 2007-04-24, 最終更新日: 2023-12-27)

主引用文献

Zhang, J.,Li, X.,Yao, B.,Shen, W.,Sun, H.,Xu, C.,Wu, J.,Shi, Y.
Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides
Biochem.Biophys.Res.Commun., 357:931-937, 2007

PubMed Abstract: Solution structure of the first Src homology (SH) 3 domain of human vinexin (V_SH3_1) was determined using nuclear magnetic resonance (NMR) method and revealed that it was a canonical SH3 domain, which has a typical beta-beta-beta-beta-alpha-beta fold. Using chemical shift perturbation and surface plasmon resonance experiments, we studied the binding properties of the SH3 domain with two different peptides from vinculin hinge regions: P856 and P868. The observations illustrated slightly different affinities of the two peptides binding to V_SH3_1. The interaction between P868 and V_SH3_1 belonged to intermediate exchange with a modest binding affinity, while the interaction between P856 and V_SH3_1 had a low binding affinity. The structure and ligand-binding interface of V_SH3_1 provide a structural basis for the further functional study of this important molecule.

PubMed: 17467669
DOI: 10.1016/j.bbrc.2007.04.029

実験手法

SOLUTION NMR