期刊
FEBS LETTERS
卷 583, 期 4, 页码 749-753出版社
WILEY
DOI: 10.1016/j.febslet.2009.01.036
关键词
Src Homology 3 domains; X-ray structure; Loop flexibility; Domain swapping; Intertwined dimer; c-Src Tyrosine kinase
资金
- Spanish Ministry of Education and Sciences [BIO2006-15517-C02-01, BIO2006-15517-C02-02]
- European Union [03-51-5569]
- Andalusian Government
Here we report the. first crystal structure of the SH3 domain of the cellular Src tyrosine kinase (c-Src-SH3) domain on its own. In the crystal two molecules of c-Src-SH3 exchange their -RT loops generating an intertwined dimer, in which the two SH3 units, preserving the binding site configuration, are oriented to allow simultaneous binding of two ligand molecules. The dimerization of c-Src-SH3 is induced, both in the crystal and in solution, by the binding of a PEG molecule at the dimer interface, indicating that this type of conformations are energetically close to the native structure. These results have important implications respect to in vivo oligomerization and amyloid aggregation. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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