Promiscuous binding nature of SH3 domains to their target proteins.

Agrawal, Vishal and Kishan, K V Radha (2002) Promiscuous binding nature of SH3 domains to their target proteins. Protein and peptide letters, 9 (3). pp. 185-93. ISSN 0929-8665

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SH3 domains are small but important domains in cell-signaling and function through protein-protein interactions. Their promiscuous nature in binding to polyproline peptides makes them much more important because many SH3 domains from different proteins bind to different proteins having polyproline template on their surface. Very subtle changes in the sequence of SH3 domains and the binding peptides determine the specificity of the peptide binding. Recent observation that SH3 domains bind to non- proline peptides makes the scenario of peptide binding involving SH3 domains complicated. If domain swapped dimerization as observed in Eps8-SH3 domain also binds different peptides, it proves the versatility of the SH3 domains in binding to peptides in various ways. An overview of the promiscuity of SH3 domains has been discussed.

Item Type: Article
Additional Information: Copyright of this article belongs to Bentham Science.
Uncontrolled Keywords: Promiscuous Binding Nature of Sh3 Domains to their Target Proteins
Subjects: Q Science > QD Chemistry
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 05 Jan 2012 15:12
Last Modified: 05 Jan 2012 15:12

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