Structure of the PI3K SH3 domain and analysis of the SH3 family.

Cell
Authors
Keywords
Abstract

Src homology 3 (SH3) domains, which are found in many proteins involved in intracellular signal transduction, mediate specific protein-protein interactions. The three-dimensional structure of the SH3 domain in the p85 subunit of the phosphatidylinositol 3-kinase (PI3K) has been determined by multidimensional NMR methods. The molecule consists of four short helices, two beta turns, and two antiparallel beta sheets. The beta sheets are highly similar to corresponding regions in the SH3 domain of the tyrosine kinase Src, even though the sequence identity of the two domains is low. There is a unique 15 amino acid insert in PI3K that contains three short helices. There are substantial differences in the identity of the amino acids that make up the receptor site of SH3 domains. The results suggest that while the overall structures of the binding sites in the PI3K and Src SH3 domains are similar, their ligand binding properties may differ.

Year of Publication
1993
Journal
Cell
Volume
72
Issue
6
Pages
945-52
Date Published
1993 Mar 26
ISSN
0092-8674
PubMed ID
7681364
Links
Grant list
GM-44993 / GM / NIGMS NIH HHS / United States