Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides

Journal Article · Fri Jun 15 00:00:00 EDT 2007 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2007.04.029· OSTI ID:20991387

Zhang, Jiahai ^[1]; Li, Xiang ^[1]; Yao, Bo ^[1]; Shen, Weiqun ^[1]; Sun, Hongbin ^[1]; Xu, Chao ^[1]; Wu, Jihui ^[1]; Shi, Yunyu ^[1]

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1. Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026 (China)

Solution structure of the first Src homology (SH) 3 domain of human vinexin (V{sub S}H3{sub 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{sub S}H3{sub 1}. The interaction between P868 and V{sub S}H3{sub 1} belonged to intermediate exchange with a modest binding affinity, while the interaction between P856 and V{sub S}H3{sub 1} had a low binding affinity. The structure and ligand-binding interface of V{sub S}H3{sub 1} provide a structural basis for the further functional study of this important molecule.

• OSTI ID: 20991387
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 4 Vol. 357; ISSN BBRCA9; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AFFINITY
CHEMICAL SHIFT
DISSOCIATION
INTERACTIONS
LIGANDS
MOLECULES
NUCLEAR MAGNETIC RESONANCE
OVERHAUSER EFFECT
PEPTIDES