TY  - JOUR
ID  - open265
UR  - http://www.benthamdirect.org/pages/b_viewarticle.php
IS  - 3
A1  - Agrawal, Vishal
A1  - Kishan, K V Radha
N2  - 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.
VL  - 9
TI  - Promiscuous binding nature of SH3 domains to their target proteins.
AV  - restricted
EP  - 93
N1  - Copyright of this article belongs to Bentham Science.
Y1  - 2002/06//
PB  - Bentham Science
JF  - Protein and peptide letters
KW  - Promiscuous Binding Nature of Sh3 Domains to their Target Proteins  

SN  - 0929-8665
SP  - 185
ER  -