Siah ubiquitin ligase is structurally related to traf and modulates tnf-α signaling. Polekhina, G., House, C., Traficante, N., Mackay, J., Relaix, F., Sassoon, D., Parker, M., & Bowtell, D. Nature Structural Biology, 9(1):68-75, 2002. cited By 115Paper doi abstract bibtex 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 Å resolution. The structure reveals that Siah is a dimeric protein and that the SBD adopts an eight-stranded β-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-α 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-α-mediated NF-κB activation. Therefore, Siah proteins share important similarities with the TRAF family of proteins, including their overall domain architecture, three-dimensional structure and functional activity. © 2002 Nature Publishing Group.
@ARTICLE{Polekhina200268,
author={Polekhina, G. and House, C.M. and Traficante, N. and Mackay, J.P. and Relaix, F. and Sassoon, D.A. and Parker, M.W. and Bowtell, D.D.L.},
title={Siah ubiquitin ligase is structurally related to traf and modulates tnf-α signaling},
journal={Nature Structural Biology},
year={2002},
volume={9},
number={1},
pages={68-75},
doi={10.1038/nsb743},
note={cited By 115},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036143826&doi=10.1038%2fnsb743&partnerID=40&md5=c995dabe69e21dac39e8e73b565c346b},
affiliation={Biota Structural Biology Laboratory, St. Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy VIC 3065, Australia; Trescowthick Research Laboratories, Peter MacCallum Cancer Institute, Locked Bag 1 A'Beckett St., Melbourne VIC 8006, Australia; Department of Biochemistry, University of Sydney, Sydney NSW 2006, Australia; Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, 1 G. Levy Place, New York NY 10029, United States; Department of Molecular Biology, Pasteur Institute, 25 rue du Dr Roux, Paris Cedex 15, France},
abstract={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 Å resolution. The structure reveals that Siah is a dimeric protein and that the SBD adopts an eight-stranded β-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-α 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-α-mediated NF-κB activation. Therefore, Siah proteins share important similarities with the TRAF family of proteins, including their overall domain architecture, three-dimensional structure and functional activity. © 2002 Nature Publishing Group.},
keywords={immunoglobulin enhancer binding protein; protein ring; protein siah; tumor necrosis factor alpha; tumor necrosis factor receptor associated death domain; tumor necrosis factor receptor associated factor; ubiquitin protein ligase; unclassified drug; zinc finger protein, amino acid sequence; article; binding site; crystal structure; enzyme structure; molecular model; molecular recognition; priority journal; protein domain; protein folding; protein protein interaction; protein structure; signal transduction; structure activity relation, Amino Acid Sequence; Animals; Binding Sites; Crystallography, X-Ray; Dimerization; Humans; Mice; Models, Molecular; Molecular Sequence Data; NF-kappa B; Nuclear Proteins; Peptide Fragments; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Proteins; Receptors, Tumor Necrosis Factor; Sequence Alignment; Sequence Homology, Amino Acid; Signal Transduction; Trans-Activation (Genetics); Tumor Necrosis Factor-alpha; Ubiquitin-Protein Ligases; Zinc; Zinc Fingers, Murinae},
issn={10728368},
pubmed_id={11742346},
language={English},
abbrev_source_title={Nat. Struct. Biol.},
document_type={Article},
source={Scopus},
}
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