Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 357, Issue: 4, Page: 931-937
2007
- 9Citations
- 9Captures
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Metrics Details
- Citations9
- Citation Indexes9
- CrossRef9
- Captures9
- Readers9
Article Description
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 β–β–β–β–α–β 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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X07007401; http://dx.doi.org/10.1016/j.bbrc.2007.04.029; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=34247880175&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17467669; https://linkinghub.elsevier.com/retrieve/pii/S0006291X07007401; https://dx.doi.org/10.1016/j.bbrc.2007.04.029
Elsevier BV
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