The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
Chembiochem. 2013 Aug 12;
Authors: Calçada EO, Felli IC, Hoek T, Pierattelli R
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.
PMID: 23940009 [PubMed - as supplied by publisher]
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Abstract
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Probing Microscopic Architecture of Opaque Heterogeneous Systems Using Double-Pulsed-Field-Gradient NMR
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Noam Shemesh, Tal Adiri and Yoram Cohen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja200303h/aop/images/medium/ja-2011-00303h_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja200303h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/W-dJo6Q8sIM
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The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
Linear Mode
