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Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.

Booker GW, Gout I, Downing AK, Driscoll PC, Boyd J, Waterfield MD, Campbell ID
Cell 73 813-22 (1993)
Cited: 119 times
EuropePMC logo PMID: 7684655

Abstract

SH3 domains are found in proteins associated with receptor tyrosine kinase signal transduction complexes. The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands. The structure is similar to that of chicken brain alpha spectrin but represents a distinct class of SH3 domain, with an insertion between the second and third beta strands that may influence binding specificity. 1H chemical shift changes induced by complex formation with a synthetic peptide derived from the SH3-binding protein dynamin, together with amino acid sequence comparisons, suggest that the ligand-binding site consists of a hydrophobic surface flanked by two charged loops.

Reviews - 1pnj mentioned but not cited (1)

  1. Somatic mutations in PI3Kalpha: structural basis for enzyme activation and drug design. Gabelli SB, Mandelker D, Schmidt-Kittler O, Vogelstein B, Amzel LM. Biochim. Biophys. Acta 1804 533-540 (2010)

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  1. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Ventura S, Zurdo J, Narayanan S, Parreño M, Mangues R, Reif B, Chiti F, Giannoni E, Dobson CM, Aviles FX, Serrano L. Proc. Natl. Acad. Sci. U.S.A. 101 7258-7263 (2004)
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