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.
Monitoring HPV-16 E7 phosphorylation events / Marcela Oliveira, N., Hosek, T., Eduardo O., C., Castiglia, F., Massimi, P., Banks, L., Felli, I.C., Pierattelli, R.. - In: VIROLOGY. - ISSN 0042-6822. - STAMPA. - 503:(2017), pp. 70-75. [10.1016/j.virol.2016.12.030]
Monitoring HPV-16 E7 phosphorylation events
Nogueira, Marcela Oliveira;Hosek, Tomas;Calçada, Eduardo O.;Felli, Isabella C.
;Pierattelli, Roberta
2017
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.
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