Journal
VIROLOGY
Volume 503, Issue -, Pages 70-75Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2016.12.030
Keywords
E7; HPV; IDP; Intrinsically Disordered Proteins; NMR; Nuclear Magnetic Resonance Spectroscopy; PTM; Phosphorylation
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Funding
- European Commission Project Marie Curie ITN IDPbyNMR [264257]
- European Commission Project BioNMR [261863]
- European Commission Project INSTRUCT [211252]
- Associazione Italiana per la Ricerca sul Cancro [14025]
- program Science without Borders of the Brazilian Ministry of Science and Technology (CNPq)
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HPV-16 E7 is one of the key proteins that, by interfering with the host metabolism through many protein protein interactions, hijacks cell regulation and contributes to malignancy. Here we report the high resolution investigation of the CR3 region of HPV-16 E7, both as an isolated domain and in the full-length protein. This opens the way to the atomic level study of the many interactions in which HPV-16 E7 is involved. Along these lines we show here the effect of one of the key post-translational modifications of HPV-16 E7, the phosphorylation by casein kinase II.
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