1abq
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(New page: 200px<br /><applet load="1abq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abq, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 08:37, 20 November 2007
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CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN
Overview
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 Structure
1ABQ is a Single protein structure of sequence from Mus musculus. 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.
Reference
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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