The Spring 2012 season of CACAO has started!
PMID:11668184
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Fazi, B, Cope, MJ, Douangamath, A, Ferracuti, S, Schirwitz, K, Zucconi, A, Drubin, DG, Wilmanns, M, Cesareni, G and Castagnoli, L (2002) Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.J. Biol. Chem. 277:5290-8
| Abstract | 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. |
| Links | PubMed Online version:10.1074/jbc.M109848200 |
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