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Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos

Nature Structural Biology volume 1, pages 891–897 (1994)Cite this article

Abstract

Src-homology 3 (SH3) domains mediate signal transduction by binding to proline-rich motifs in target proteins. We have determined the high-resolution NMR structure of the complex between the amino-terminal SH3 domain of GRB2 and a ten amino acid peptide derived from the guanine nucleotide releasing factor Sos. The NMR data show that the peptide adopts the conformation of a left-handed polyproline type II helix and interacts with three major sites on the SH3 domain. The orientation of the bound peptide is opposite to that of proline-rich peptides bound to the SH3 domains of AbI, Fyn and p85.

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Authors and Affiliations

  1. Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science, 3-18-22, Honkomagome, Bunkyo-ku, Tokyo, 113, Japan

    Hiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Shigeo Tsuchiya, Kenji Ogura, Koji Nagata & Fuyuhiko Inagaki

  2. Molecular Biology Research Lab, Daiichi Pharmaceutical Co., Ltd., 16-13, Kitakasai 1-chome, Edogawa ku, Tokyo, 134, Japan

    Hiroaki Terasawa

  3. Laboratory of Molecular Genetics, The Tsukuba Life Science Center, RIKEN, 3-1-1, Koyadai, Tsukubashi, Ibaraki, 305, Japan

    Shunsuke Ishii

  4. Department of Pharmacology, New York University Medical Center, New York, New York, 10016, USA

    Valsan Mandiyan & Joseph Schlessinger

  5. Max-Planck Institut für Biochemie, 8033 Am Klopfrspitz 18A, Martinsried, Germany

    Axel Ullrich & Fuyuhiko Inagaki

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  1. Hiroaki Terasawa
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Terasawa, H., Kohda, D., Hatanaka, H. et al. Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos. Nat Struct Mol Biol 1, 891–897 (1994). https://doi.org/10.1038/nsb1294-891

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