Monitoring HPV-16 E7 phosphorylation events

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Casein Kinase II / metabolism*
  • Cell Line
  • Human papillomavirus 16 / metabolism*
  • Humans
  • Neoplasms / pathology*
  • Nuclear Magnetic Resonance, Biomolecular
  • Papillomavirus E7 Proteins / metabolism*
  • Phosphorylation
  • Protein Interaction Domains and Motifs
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary

Substances

  • Papillomavirus E7 Proteins
  • oncogene protein E7, Human papillomavirus type 16
  • Casein Kinase II