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

Musacchio A, Saraste M, Wilmanns M
Nat Struct Biol 1 546-51 (1994)
Related entries: 1abo, 1abq

Cited: 189 times
EuropePMC logo PMID: 7664083

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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