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 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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Bibliographic Details
Main Authors: Katia Zanier, Christina Stutz, Susanne Kintscher, Eileen Reinz, Peter Sehr, Julia Bulkescher, Karin Hoppe-Seyler, Gilles Travé, Felix Hoppe-Seyler
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4226571?pdf=render

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http://europepmc.org/articles/PMC4226571?pdf=render

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