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Peptide inhibitors of src SH3-SH2-phosphoprotein interactions.

Gilmer T, Rodriguez M, Jordan S, Crosby R, Alligood K, Green M, Kimery M, Wagner C, Kinder D, Charifson P
J Biol Chem 269 31711-9 (1994)
Cited: 80 times
EuropePMC logo PMID: 7527393

Abstract

Activated pp60c-src has been implicated in a number of human malignancies including colon carcinoma and breast adenocarcinoma. Association of the src SH2 domain with tyrosine-phosphorylated proteins plays a role in src-mediated signal transduction. Inhibitors of src SH2 domain-phosphoprotein interactions are, thus, of great interest in defining the role(s) of src in signal transduction pathways. To facilitate such studies, an enzyme-linked immunosorbent assay (ELISA) was developed to detect inhibitors of src SH2-phosphoprotein interactions. This assay measures inhibition of binding of a fusion construct (glutathione S-transferase src SH3-SH2) with autophosphorylated epidermal growth factor receptor tyrosine kinase domain. Activities of phosphopeptide segments derived from potential src SH2 cognate phosphoprotein partners were determined, with the focal adhesion kinase-derived segment VSETDDY*AEIIDE yielding the highest inhibitory activity. Structure activity studies starting from acetyl (Ac)-Y*EEIE have identified Ac-Y*Y*Y*IE as the most active compound screened in the ELISA. This compound is at least 20-fold more active than the parent peptide Ac-Y*EEIE. A high resolution (2 A) crystal structure of human src SH2 complexed with Ac-Y*EEIE was obtained and provided a useful framework for understanding the structure-activity relationships. Additionally, Ac-Y*EEIE was able to block interactions between src and its cellular phosphoprotein partners in vanadate-treated cell lysates from MDA-MB-468 breast carcinoma cells. However, it is unable to abrogate proliferation of MDA-MB-468 cells in culture, presumably because of poor cell penetration and/or lability of the phosphate group on tyrosine.

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Articles - 1shd mentioned but not cited (4)

  1. Quantitative prediction of protein-protein binding affinity with a potential of mean force considering volume correction. Su Y, Zhou A, Xia X, Li W, Sun Z. Protein Sci 18 2550-2558 (2009)
  2. Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains. Zhou HX. Biophys. J. 91 3170-3181 (2006)
  3. Binding modes of peptidomimetics designed to inhibit STAT3. Dhanik A, McMurray JS, Kavraki LE. PLoS ONE 7 e51603 (2012)
  4. Computational protein design: validation and possible relevance as a tool for homology searching and fold recognition. Schmidt Am Busch M, Sedano A, Simonson T. PLoS ONE 5 e10410 (2010)


Reviews citing this publication (13)

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Articles citing this publication (61)

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