1k2f
From Proteopedia
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siah, Seven In Absentia Homolog
Overview
Members of the Siah (seven in absentia homolog) family of RING domain, proteins are components of E3 ubiquitin ligase complexes that catalyze, ubiquitination of proteins. We have determined the crystal structure of, the substrate-binding domain (SBD) of murine Siah1a to 2.6 A resolution., The structure reveals that Siah is a dimeric protein and that the SBD, adopts an eight-stranded beta-sandwich fold that is highly similar to the, TRAF-C region of TRAF (TNF-receptor associated factor) proteins. The, TRAF-C region interacts with TNF-alpha receptors and TNF-receptor, associated death-domain (TRADD) proteins; however, our findings indicate, that these interactions are unlikely to be mimicked by Siah. The Siah, structure also reveals two novel zinc fingers in a region with sequence, similarity to TRAF. We find that the Siah1a SBD potentiates, TNF-alpha-mediated NF-kappa B activation. Therefore, Siah proteins share, important similarities with the TRAF family of proteins, including their, overall domain architecture, three-dimensional structure and functional, activity.
About this Structure
1K2F is a Single protein structure of sequence from Mus musculus with ZN and BME as ligands. Full crystallographic information is available from OCA.
Reference
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling., Polekhina G, House CM, Traficante N, Mackay JP, Relaix F, Sassoon DA, Parker MW, Bowtell DD, Nat Struct Biol. 2002 Jan;9(1):68-75. PMID:11742346
Page seeded by OCA on Tue Nov 20 18:47:36 2007
