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Article

Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53.

Structure (London, England : 1993) - 4 Apr 2012

Zanier Katia, ould M'hamed ould Sidi Abdellahi, Boulade-Ladame Charlotte, Rybin Vladimir, Chappelle Anne, Atkinson Andrew, Kieffer Bruno, Travé Gilles

Abstract excerpt

The viral oncoprotein E6 is an essential factor for cervical cancers induced by "high-risk" mucosal HPV. Among other oncogenic activities, E6 recruits the ubiquitin ligase E6AP to promote the ubiquitination and subsequent proteasomal degradation of p53. E6 is prone to self-association, which long precluded its structural analysis. Here we found that E6 specifically dimerizes through its N-terminal domain and that...

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Share to Nuclear Magnetic Resonance, Biomolecular
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22483108
DOI: 10.1016/j.str.2012.02.001
PMCID: PMC3325491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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