Monitoring HPV-16 E7 phosphorylation events

Journal Article · Wed Mar 15 00:00:00 EDT 2017 · Virology

DOI:https://doi.org/10.1016/J.VIROL.2016.12.030· OSTI ID:22692244

Nogueira, Marcela O.; Hošek, Tomáš; Calçada, Eduardo O.; Castiglia, Francesca ^[1]; Massimi, Paola; Banks, Lawrence ^[2]; Pierattelli, Roberta ^[1]

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1. Magnetic Resonance Center (CERM) and Department of Chemistry “Ugo Schiff”, University of Florence, via Luigi Sacconi 6, Sesto Fiorentino (Italy)
2. International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, Trieste (Italy)

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.

• OSTI ID: 22692244
• Journal Information: Virology, Vol. 503; Other Information: Copyright (c) 2017 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CASEIN
METABOLISM
NEOPLASMS
NUCLEAR MAGNETIC RESONANCE
PHOSPHORYLATION
PHOSPHOTRANSFERASES
SPECTROSCOPY