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- W2042531119 abstract "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 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." @default.
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- W2042531119 date "2007-06-01" @default.
- W2042531119 modified "2023-09-25" @default.
- W2042531119 title "Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides" @default.
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- W2042531119 doi "https://doi.org/10.1016/j.bbrc.2007.04.029" @default.
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