1VCB

THE VHL-ELONGINC-ELONGINB STRUCTURE

Summary for 1VCB

• Entry DOI: 10.2210/pdb1vcb/pdb
• Descriptor: PROTEIN (ELONGIN B), PROTEIN (ELONGIN C), PROTEIN (VHL), ... (4 entities in total)
• Functional Keywords: tumor suppressor, cancer, ubiquitin, beta sandwich, transcription, transcriptional elongation
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (Probable): Q15370 Q15369; Isoform 1: Cytoplasm. Isoform 3: Cytoplasm: P40337
• Total number of polymer chains: 12
• Total formula weight: 176764.31

Authors

Stebbins, C.E.,Kaelin, W.G.,Pavletich, N.P. (deposition date: 1999-03-13, release date: 1999-04-21, Last modification date: 2023-12-27)

Primary citation

Stebbins, C.E.,Kaelin Jr., W.G.,Pavletich, N.P.
Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.
Science, 284:455-461, 1999

PubMed Abstract: 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.

PubMed: 10205047
DOI: 10.1126/science.284.5413.455

Experimental method

X-RAY DIFFRACTION (2.7 Å)