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Nat Struct Biol. 1994 Apr;1(4):221-5.

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

Author information

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

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.

PMID:
7656049
DOI:
10.1038/nsb0494-221
[Indexed for MEDLINE]

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