Theoretical 3D Structures of All SH3 Domains from Nck-1 and Nck-2

Abstract

Nck-1 and Nck-2 are ubiquitously expressed a Src homology 2 (SH2)- and three SH3-domaincontaining adaptor proteins that interact with numerous signal transduction proteins. To elucidate the structure of SH3 domains from Ncks, we turned to use Bioinformatics method to understand the properties of each individual SH3 domains. The results showed that whole Nck1 and Nck2 share about 68% sequence identity, however, homologous domains have very strong identity: 82% for SH3-1, 80% for SH3-2, and 73% for SH3-3. Theoretical structures of SH3 domains are obtained from homology modeling. These structures showed the difference of residues distributing in the binding sites and also difference in charge distribution in the surface of each SH3 domains. Our data could be implied that each SH3 domain binds to different ligands which could be useful for further studying of ligand interaction with this domains.