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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2002-2-11
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ABF1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/PRK1 protein, Petunia inflata,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/cbp1 protein, S pombe
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5290-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11668184-Actins,
pubmed-meshheading:11668184-Amino Acid Motifs,
pubmed-meshheading:11668184-Amino Acid Sequence,
pubmed-meshheading:11668184-Binding Sites,
pubmed-meshheading:11668184-Cytoskeleton,
pubmed-meshheading:11668184-DNA-Binding Proteins,
pubmed-meshheading:11668184-Endocytosis,
pubmed-meshheading:11668184-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:11668184-Gene Library,
pubmed-meshheading:11668184-Ligands,
pubmed-meshheading:11668184-Models, Biological,
pubmed-meshheading:11668184-Models, Molecular,
pubmed-meshheading:11668184-Molecular Sequence Data,
pubmed-meshheading:11668184-Mutagenesis, Site-Directed,
pubmed-meshheading:11668184-Peptide Library,
pubmed-meshheading:11668184-Peptides,
pubmed-meshheading:11668184-Plant Proteins,
pubmed-meshheading:11668184-Plasmids,
pubmed-meshheading:11668184-Protein Binding,
pubmed-meshheading:11668184-Protein Conformation,
pubmed-meshheading:11668184-Protein Structure, Tertiary,
pubmed-meshheading:11668184-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:11668184-Saccharomyces cerevisiae,
pubmed-meshheading:11668184-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11668184-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:11668184-Structure-Activity Relationship,
pubmed-meshheading:11668184-Transcription Factors,
pubmed-meshheading:11668184-Two-Hybrid System Techniques,
pubmed-meshheading:11668184-src Homology Domains
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pubmed:year |
2002
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pubmed:articleTitle |
Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.
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pubmed:affiliation |
Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Roma, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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