2an6
From Proteopedia
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'''Protein-peptide complex''' | '''Protein-peptide complex''' | ||
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[[Category: Parker, M W.]] | [[Category: Parker, M W.]] | ||
[[Category: Polekhina, G.]] | [[Category: Polekhina, G.]] | ||
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Revision as of 16:14, 3 May 2008
Protein-peptide complex
Overview
The Siah family of RING proteins function as ubiquitin ligase components, contributing to the degradation of multiple targets involved in cell growth, differentiation, angiogenesis, oncogenesis, and inflammation. Previously, a binding motif (degron) was recognized in many of the Siah degradation targets, suggesting that Siah itself may facilitate substrate recognition. We report the crystal structure of the Siah in complex with a peptide containing the degron motif. Binding is within a groove formed in part by the zinc fingers and the first two beta strands of the TRAF-C domain of Siah. We show that residues in the degron, previously described to facilitate binding to Siah, interact with the protein. Mutagenesis of Siah at sites of interaction also abrogates both in vitro peptide binding and destabilization of a known Siah target.
About this Structure
2AN6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Elucidation of the substrate binding site of Siah ubiquitin ligase., House CM, Hancock NC, Moller A, Cromer BA, Fedorov V, Bowtell DD, Parker MW, Polekhina G, Structure. 2006 Apr;14(4):695-701. PMID:16615911 Page seeded by OCA on Sat May 3 19:14:40 2008
