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1k2f

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{{STRUCTURE_1k2f| PDB=1k2f | SCENE= }}
{{STRUCTURE_1k2f| PDB=1k2f | SCENE= }}
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'''siah, Seven In Absentia Homolog'''
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===siah, Seven In Absentia Homolog===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11742346 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11742346}}
==About this Structure==
==About this Structure==
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[[Category: Traficante, N.]]
[[Category: Traficante, N.]]
[[Category: Beta-sandwich]]
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Revision as of 18:30, 1 July 2008

Image:1k2f.png

Template:STRUCTURE 1k2f

siah, Seven In Absentia Homolog

Template:ABSTRACT PUBMED 11742346

About this Structure

1K2F is a Single protein structure of sequence from Mus musculus. 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

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