1k2f
From Proteopedia
(New page: 200px<br /><applet load="1k2f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k2f, resolution 2.6Å" /> '''siah, Seven In Absent...) |
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| - | [[Image:1k2f.jpg|left|200px]]<br /><applet load="1k2f" size=" | + | [[Image:1k2f.jpg|left|200px]]<br /><applet load="1k2f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k2f, resolution 2.6Å" /> | caption="1k2f, resolution 2.6Å" /> | ||
'''siah, Seven In Absentia Homolog'''<br /> | '''siah, Seven In Absentia Homolog'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Members of the Siah (seven in absentia homolog) family of RING domain | + | 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== | ==About this Structure== | ||
| - | 1K2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bowtell, D | + | [[Category: Bowtell, D D.L.]] |
| - | [[Category: House, C | + | [[Category: House, C M.]] |
| - | [[Category: Mackay, J | + | [[Category: Mackay, J P.]] |
| - | [[Category: Parker, M | + | [[Category: Parker, M W.]] |
[[Category: Polekhina, G.]] | [[Category: Polekhina, G.]] | ||
[[Category: Relaix, F.]] | [[Category: Relaix, F.]] | ||
| - | [[Category: Sassoon, D | + | [[Category: Sassoon, D A.]] |
[[Category: Traficante, N.]] | [[Category: Traficante, N.]] | ||
[[Category: BME]] | [[Category: BME]] | ||
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[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:26 2008'' |
Revision as of 11:29, 21 February 2008
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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 and 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
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