| Literature DB >> 28126639 |
Marcela O Nogueira1, Tomáš Hošek1, Eduardo O Calçada1, Francesca Castiglia1, Paola Massimi2, Lawrence Banks2, Isabella C Felli3, Roberta Pierattelli4.
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.Entities:
Keywords: E7; HPV; IDP; Intrinsically Disordered Proteins; NMR; Nuclear Magnetic Resonance Spectroscopy; PTM; Phosphorylation
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Year: 2017 PMID: 28126639 DOI: 10.1016/j.virol.2016.12.030
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616