Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides |
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Authors: | Zhang Jiahai Li Xiang Yao Bo Shen Weiqun Sun Hongbin Xu Chao Wu Jihui Shi Yunyu |
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Institution: | Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China. |
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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. |
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Keywords: | SH3 Src homology 3 2D and 3D two- and three-dimensional NMR nuclear magnetic resonance HSQC heteronuclear single quantum correlation NOE nuclear Overhauser effect RMSD root mean-square deviation Kd dissociation constant |
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