1jo8: Difference between revisions
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|PDB= 1jo8 |SIZE=350|CAPTION= <scene name='initialview01'>1jo8</scene>, resolution 1.30Å | |PDB= 1jo8 |SIZE=350|CAPTION= <scene name='initialview01'>1jo8</scene>, resolution 1.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo8 OCA], [http://www.ebi.ac.uk/pdbsum/1jo8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jo8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:36 2008'' | ||
Revision as of 21:36, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural analysis of the yeast actin binding protein Abp1 SH3 domain
OverviewOverview
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 StructureAbout this Structure
1JO8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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
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