The E6AP Binding Pocket of the HPV16 E6 Oncoprotein Provides a Docking Site for a Small Inhibitory Peptide Unrelated to E6AP, Indicating Druggability of E6

The HPV E6 oncoprotein maintains the malignant phenotype of HPV-positive cancer cells and represents an attractive therapeutic target. E6 forms a complex with the cellular E6AP ubiquitin ligase, ultimately leading to p53 degradation. The recently elucidated x-ray structure of a HPV16 E6/E6AP complex...

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Опубликовано в: :PLoS One
Главные авторы: Zanier, Katia, Stutz, Christina, Kintscher, Susanne, Reinz, Eileen, Sehr, Peter, Bulkescher, Julia, Hoppe-Seyler, Karin, Travé, Gilles, Hoppe-Seyler, Felix
Формат: Artigo
Язык:Inglês
Опубликовано: Public Library of Science 2014
Предметы:
Research Article
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC4226571/
https://ncbi.nlm.nih.gov/pubmed/25383876
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0112514
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