1oby: Difference between revisions
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Revision as of 19:24, 12 November 2007
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CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.
OverviewOverview
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, revision of their classification and of the existing model of their, mechanism.
About this StructureAbout this Structure
1OBY is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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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