2btt Citations

New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.

Abstract

SH3 domains are small protein modules that are involved in protein-protein interactions in several essential metabolic pathways. The availability of the complete genome and the limited number of clearly identifiable SH3 domains make the yeast Saccharomyces cerevisae an ideal proteomic-based model system to investigate the structural rules dictating the SH3-mediated protein interactions and to develop new tools to assist these studies. In the present work, we have determined the solution structure of the SH3 domain from Myo3 and modeled by homology that of the highly homologous Myo5, two myosins implicated in actin polymerization. We have then implemented an integrated approach that makes use of experimental and computational methods to characterize their binding properties. While accommodating their targets in the classical groove, the two domains have selectivity in both orientation and sequence specificity of the target peptides. From our study, we propose a consensus sequence that may provide a useful guideline to identify new natural partners and suggest a strategy of more general applicability that may be of use in other structural proteomic studies.

Reviews citing this publication (4)

  1. Analyzing protein interaction networks using structural information. Kiel C, Beltrao P, Serrano L. Annu. Rev. Biochem. 77 415-441 (2008)
  2. SH3 domains: modules of protein-protein interactions. Kurochkina N, Guha U. Biophys Rev 5 29-39 (2013)
  3. SH3 domains: modules of protein-protein interactions. Kurochkina N, Guha U. Biophys Rev 5 29-39 (2013)
  4. Analyzing protein interaction networks using structural information. Kiel C, Beltrao P, Serrano L. Annu. Rev. Biochem. 77 415-441 (2008)

Articles citing this publication (5)

  1. A unified conformational selection and induced fit approach to protein-peptide docking. Trellet M, Melquiond AS, Bonvin AM. PLoS ONE 8 e58769 (2013)
  2. Structure-based prediction of the Saccharomyces cerevisiae SH3-ligand interactions. Fernandez-Ballester G, Beltrao P, Gonzalez JM, Song YH, Wilmanns M, Valencia A, Serrano L. J. Mol. Biol. 388 902-916 (2009)
  3. Paxillin and ponsin interact in nascent costameres of muscle cells. Gehmlich K, Pinotsis N, Hayess K, van der Ven PF, Milting H, El Banayosy A, Körfer R, Wilmanns M, Ehler E, Fürst DO. J. Mol. Biol. 369 665-682 (2007)
  4. Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain. Hwang KJ, Mahmoodian F, Ferretti JA, Korn ED, Gruschus JM. Proc. Natl. Acad. Sci. U.S.A. 104 784-789 (2007)
  5. o-Nitrotyrosine and p-iodophenylalanine as spectroscopic probes for structural characterization of SH3 complexes. De Filippis V, Draghi A, Frasson R, Grandi C, Musi V, Fontana A, Pastore A. Protein Sci. 16 1257-1265 (2007)