1lm8: Difference between revisions
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{{STRUCTURE_1lm8| PDB=1lm8 | SCENE= }} | |||
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'''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex''' | '''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex''' | ||
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[[Category: Pavletich, N P.]] | [[Category: Pavletich, N P.]] | ||
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: | [[Category: Oxygen sensing]] | ||
[[Category: | [[Category: Regulation]] | ||
[[Category: | [[Category: Tumor suppressor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:03:34 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 21:03, 2 May 2008
Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
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.
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 Sat May 3 00:03:34 2008
