1abo
CRYSTAL STRUCTURE OF THE COMPLEX OF THE ABL TYROSINE KINASE SH3 DOMAIN WITH 3BP-1 SYNTHETIC PEPTIDE
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OverviewOverview
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.
About this StructureAbout this Structure
1ABO is a Protein complex structure of sequences from Mus musculus with SO4 as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides., Musacchio A, Saraste M, Wilmanns M, Nat Struct Biol. 1994 Aug;1(8):546-51. PMID:7664083
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