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- W1620032110 abstract "Human papillomavirus (HPV) E6 protein can inactivate tumor suppressor p53 by inducing its degradation. We now find that high-risk HPV E6 binds to p53 at two distinct sites; one is within the core structure of p53, and another is at the C terminus of p53. Binding to the core of p53 is required for E6-mediated degradation, as shown by deletion analysis and the properties of a point mutant at residue 135. Both low- and high-risk HPV E6 can bind to a C-terminal region of p53, but these interactions do not induce degradation. These results resolve previous seemingly contradictory findings that attributed the distinctive functional properties of high- and low-risk E6 proteins to either a difference in their abilities to associate with p53 or a difference in their N-terminal structures." @default.
- W1620032110 created "2016-06-24" @default.
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- W1620032110 date "1996-07-01" @default.
- W1620032110 modified "2023-10-16" @default.
- W1620032110 title "High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradation" @default.
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- W1620032110 doi "https://doi.org/10.1128/jvi.70.7.4509-4516.1996" @default.
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