The heterogeneous structural behavior of E7 from HPV16 revealed by NMR spectroscopy.
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.
Magnetic Resonance Center (CERM), University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino (Italy).
Eduardo O
EO
Calçada
Isabella C
IC
Felli
Tomáš
T
Hošek
Roberta
R
Pierattelli
D000595:Amino Acid Sequence; D052162:Human papillomavirus 16 / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D050725:Papillomavirus E7 Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D013696:Temperature
D050725:Papillomavirus E7 Proteins; D011994:Recombinant Proteins; C059731:oncogene protein E7, Human papillomavirus type 16
HPV; IDP; heteronuclear NMR; viral proteins