1lm8
From Proteopedia
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| - | [[Image:1lm8.gif|left|200px]] | + | [[Image:1lm8.gif|left|200px]] |
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| - | '''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex''' | + | {{Structure |
| + | |PDB= 1lm8 |SIZE=350|CAPTION= <scene name='initialview01'>1lm8</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LM8 is a [ | + | 1LM8 is a [[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=1LM8 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling., Min JH, Yang H, Ivan M, Gertler F, Kaelin WG Jr, Pavletich NP, Science. 2002 Jun 7;296(5574):1886-9. Epub 2002 May 9. PMID:[http:// | + | Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling., Min JH, Yang H, Ivan M, Gertler F, Kaelin WG Jr, Pavletich NP, Science. 2002 Jun 7;296(5574):1886-9. Epub 2002 May 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12004076 12004076] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: tumor suppressor]] | [[Category: tumor suppressor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:28 2008'' |
Revision as of 10:32, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
Contents |
Overview
The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling.
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
1LM8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling., Min JH, Yang H, Ivan M, Gertler F, Kaelin WG Jr, Pavletich NP, Science. 2002 Jun 7;296(5574):1886-9. Epub 2002 May 9. PMID:12004076
Page seeded by OCA on Thu Mar 20 12:32:28 2008
