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Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition

Nature Structural Biology volume 1, pages 221–225 (1994)Cite this article

Abstract

Src homology 3 (SH3) domains bind specific proline-rich peptide motifs. To identify interactions involved in peptide recognition, we have mutated residues on the putative binding surface of an SH3 domain from the Caenorhabditis elegans protein Sem-5. Among the most critical positions are three adjacent aromatic residues, which appear to participate in highly stereospecific packing interactions with the ligand. The co-planar arrangement of two of these residues closely matches the periodicity of a poly-proline II (PPII) helix. Thus, a model for recognition has the peptide adopting a PPII helix, with the pyrrolidine rings on one helical face interlocking with the aromatic SH3 residues.

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Authors and Affiliations

  1. Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, Connecticut, 06511, USA

    Wendell A. Lim & Frederic M. Richards

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  1. Wendell A. Lim
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Lim, W., Richards, F. Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nat Struct Mol Biol 1, 221–225 (1994). https://doi.org/10.1038/nsb0494-221

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