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| {{STRUCTURE_1jo8| PDB=1jo8 | SCENE= }} | | {{STRUCTURE_1jo8| PDB=1jo8 | SCENE= }} |
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| '''Structural analysis of the yeast actin binding protein Abp1 SH3 domain'''
| | ===Structural analysis of the yeast actin binding protein Abp1 SH3 domain=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11668184}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11668184 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11668184}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zucconi, A.]] | | [[Category: Zucconi, A.]] |
| [[Category: Sh3 domain actin-binding-protein]] | | [[Category: Sh3 domain actin-binding-protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:29:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:32:52 2008'' |
