The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy |
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| Authors: | Eduardo O Calçada Prof Isabella C Felli Tomá? Ho?ek Prof Roberta Pierattelli |
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| Affiliation: | 1. Magnetic Resonance Center (CERM), University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino (Italy);2. Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino (Italy) |
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| Abstract: | 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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| Keywords: | heteronuclear NMR HPV IDP viral proteins |
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