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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-08

AUTHORS

Andrea Musacchio, Matti Saraste, Matthias Wilmanns

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. More... »

PAGES

546-551

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0894-546

DOI

http://dx.doi.org/10.1038/nsb0894-546

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037549643

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7664083


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