1jo8
From Proteopedia
|
Structural analysis of the yeast actin binding protein Abp1 SH3 domain
Overview
Abp1p is an actin-binding protein that plays a central role in the, organization of Saccharomyces cerevisiae actin cytoskeleton. By a, combination of two-hybrid and phage-display approaches, we have identified, six new ligands of the Abp1-SH3 domain. None of these SH3-mediated novel, interactions was detected in recent all genome high throughput protein, interaction projects. Here we show that the SH3-mediated association of, Abp1p with the Ser/Thr kinases Prk1p and Ark1p is essential for their, localization to actin cortical patches. The Abp1-SH3 domain has a rather, unusual binding specificity, because its target peptides contain the, tetrapentapeptide +XXXPXXPX+PXXL with positive charges flanking the, polyproline core on both sides. Here we present the structure of the, Abp1-SH3 domain solved at 1.3-A resolution. The peptide-binding pockets in, the SH3 domain are flanked by two acidic residues that are uncommon at, those positions in the SH3 domain family. We have shown by site-directed, mutagenesis that one of these negatively charged side chains may be the, key determinant for the preference for non-classical ligands.
About this Structure
1JO8 is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis., Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L, J Biol Chem. 2002 Feb 15;277(7):5290-8. Epub 2001 Oct 19. PMID:11668184
Page seeded by OCA on Tue Nov 20 18:25:05 2007
