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High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides

Nature Structural Biology volume 1, pages 546–551 (1994)Cite this article

Abstract

Src-homology 3 (SH3) domains bind to proline-rich motifs in target proteins. We have determined high-resolution crystal structures of the complexes between the SH3 domains of Abl and Fyn tyrosine kinases, and two ten-residue proline-rich peptides derived from the SH3-binding proteins 3BP-1 and 3BP-2. The X-ray data show that the basic mode of binding of both proline-rich peptides is the same. Peptides are bound over their entire length and interact with three major sites on the SH3 molecules by both hydrogen-bonding and van der Waals contacts. Residues 4-10 of the peptide adopt the conformation of a left-handed polyproline helix type II. Binding of the proline at position 2 requires a kink at the non-proline position 3.

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Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 102209, D-69012, Heidelberg, Germany

    Andrea Musacchio, Matti Saraste & Matthias Wilmanns

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  1. Andrea Musacchio
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  2. Matti Saraste
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  3. Matthias Wilmanns
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Musacchio, A., Saraste, M. & Wilmanns, M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat Struct Mol Biol 1, 546–551 (1994). https://doi.org/10.1038/nsb0894-546

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