2NWM

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

Summary for 2NWM

• Entry DOI: 10.2210/pdb2nwm/pdb
• Descriptor: Vinexin (1 entity in total)
• Functional Keywords: vinexin sh3 domain, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Isoform Alpha: Cell junction (By similarity). Isoform Beta: Cell junction (By similarity): O60504
• Total number of polymer chains: 1
• Total formula weight: 7688.76

Authors

Zhang, J.,Yao, B.,Wu, J.,Shi, Y. (deposition date: 2006-11-15, release date: 2007-04-24, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

SOLUTION NMR