1obz
From Proteopedia
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Revision as of 13:44, 30 October 2007
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CRYSTAL STRUCTURE OF THE COMPLEX OF THE PDZ TANDEM OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
Overview
Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5, receptor (alpha chain) and syndecan, reveal the molecular roots of, syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function, in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither, mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the, syndecan interaction as class II (-phi-X-phi). These results, in, conjunction with other emerging structural data on PDZ domains, call for a, ... [(full description)]
About this Structure
1OBZ is a [Protein complex] structure of sequences from [Homo sapiens] with ACT as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm., Kang BS, Cooper DR, Devedjiev Y, Derewenda U, Derewenda ZS, Structure. 2003 Jul;11(7):845-53. PMID:12842047
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