1jo8: Difference between revisions

Revision as of 14:24, 21 February 2008

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 with as ligand. 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

Page seeded by OCA on Thu Feb 21 13:24:48 2008

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OCA

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-[[Image:1jo8.jpg|left|200px]]<br /><applet load="1jo8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jo8.jpg|left|200px]]<br /><applet load="1jo8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jo8, resolution 1.30&Aring;" />
 '''Structural analysis of the yeast actin binding protein Abp1 SH3 domain'''<br />
 ==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.
+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==
-JO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JO8 OCA].
+JO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO8 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Castagnoli, L.]]
 [[Category: Cesareni, G.]]
-[[Category: Cope, M.J.]]
+[[Category: Cope, M J.]]
 [[Category: Douangamath, A.]]
-[[Category: Drubin, D.G.]]
+[[Category: Drubin, D G.]]
 [[Category: Fazi, B.]]
 [[Category: Ferracuti, S.]]
@@ Line 26: / Line 26: @@
 [[Category: sh3 domain actin-binding-protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:25:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:48 2008''