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Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.

http://www.ncbi.nlm.nih.gov/pubmed/11668184

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.

Pubmed ID: 11668184 RIS Download

Mesh terms: Actins | Amino Acid Motifs | Amino Acid Sequence | Binding Sites | Cytoskeleton | DNA-Binding Proteins | Endocytosis | Enzyme-Linked Immunosorbent Assay | Gene Library | Ligands | Models, Biological | Models, Molecular | Molecular Sequence Data | Mutagenesis, Site-Directed | Peptide Library | Peptides | Plant Proteins | Plasmids | Protein Binding | Protein Conformation | Protein Structure, Tertiary | Receptor Protein-Tyrosine Kinases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Schizosaccharomyces pombe Proteins | Structure-Activity Relationship | Transcription Factors | Two-Hybrid System Techniques | src Homology Domains

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM42759
  • Agency: NIGMS NIH HHS, Id: GM50399

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