1vcb
From Proteopedia
(New page: 200px<br /> <applet load="1vcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vcb, resolution 2.7Å" /> '''THE VHL-ELONGINC-ELO...) |
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| - | [[Image:1vcb.gif|left|200px]]<br /> | + | [[Image:1vcb.gif|left|200px]]<br /><applet load="1vcb" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1vcb, resolution 2.7Å" /> | caption="1vcb, resolution 2.7Å" /> | ||
'''THE VHL-ELONGINC-ELONGINB STRUCTURE'''<br /> | '''THE VHL-ELONGINC-ELONGINB STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mutation of the VHL tumor suppressor is associated with the inherited von | + | Mutation of the VHL tumor suppressor is associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site. The structure extends the similarities to the SCF (Skp1-Cul1-F-box protein) complex that targets proteins for degradation, supporting the hypothesis that VHL may function in an analogous pathway. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VCB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1VCB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Kaelin, W | + | [[Category: Kaelin, W G.]] |
| - | [[Category: Pavletich, N | + | [[Category: Pavletich, N P.]] |
| - | [[Category: Stebbins, C | + | [[Category: Stebbins, C E.]] |
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: cancer]] | [[Category: cancer]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:48 2008'' |
Revision as of 13:33, 21 February 2008
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THE VHL-ELONGINC-ELONGINB STRUCTURE
Contents |
Overview
Mutation of the VHL tumor suppressor is associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site. The structure extends the similarities to the SCF (Skp1-Cul1-F-box protein) complex that targets proteins for degradation, supporting the hypothesis that VHL may function in an analogous pathway.
Disease
Known diseases associated with this structure: Hemangioblastoma, cerebellar, somatic OMIM:[608537], Pheochromocytoma OMIM:[608537], Polycythemia, benign familial OMIM:[608537], Renal cell carcinoma, somatic OMIM:[608537], von Hippel-Lindau syndrome OMIM:[608537]
About this Structure
1VCB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function., Stebbins CE, Kaelin WG Jr, Pavletich NP, Science. 1999 Apr 16;284(5413):455-61. PMID:10205047
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