4.4 Article

The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy

Journal

CHEMBIOCHEM
Volume 14, Issue 14, Pages 1876-1882

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201300172

Keywords

heteronuclear NMR; HPV; IDP; viral proteins

Funding

  1. Joint Research Activity and Access to Research Infrastructures (BioNMR) [261863]
  2. Marie Curie ITN programs (IDPbyNMR) in the EC 7th Framework [264257]

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The E7 protein from human papillomavirus (HPV) plays a key role in oncogenesis; for this reason, it is a target of great biomedical interest. To date, no high resolution information is available for the full protein. We present here the NMR characterization of the entire E7 from HPV16, one of the most oncogenic variants of the virus. The protein is very heterogeneous in terms of structural and dynamic properties with a highly flexible N-terminal module and a more structured C terminus. This opens possibilities for studies of molecular-level interactions and post-translational modifications of the protein to unravel functional details that might be linked to its highly oncogenic potential.

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