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. 2017 Mar:503:70-75.
doi: 10.1016/j.virol.2016.12.030. Epub 2017 Jan 23.

Monitoring HPV-16 E7 phosphorylation events

Marcela O Nogueira  1 , Tomáš Hošek  1 , Eduardo O Calçada  1 , Francesca Castiglia  1 , Paola Massimi  2 , Lawrence Banks  2 , Isabella C Felli  3 , Roberta Pierattelli  4
Affiliations
Free article

Monitoring HPV-16 E7 phosphorylation events

Marcela O Nogueira et al. Virology. 2017 Mar.
Free article

Abstract

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.

Keywords: E7; HPV; IDP; Intrinsically Disordered Proteins; NMR; Nuclear Magnetic Resonance Spectroscopy; PTM; Phosphorylation.

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