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...
Furkejuvvon:
| Váldodahkkit: | , , , , , , , , |
|---|---|
| Materiálatiipa: | Artigo |
| Giella: | Inglês |
| Almmustuhtton: |
Public Library of Science (PLoS)
2014-01-01
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| Ráidu: | PLoS ONE |
| Liŋkkat: | http://europepmc.org/articles/PMC4226571?pdf=render |
| Fáddágilkorat: |
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