Structure of the full-length HCV IRES in solution

Abstract : The 5'-untranslated region of the hepatitis C virus genome contains an internal ribosome entry site (IRES) that initiates cap-independent translation of the viral RNA. Until now, the structural characterization of the entire (IRES) remained limited to cryo-electron microscopy reconstructions of the (IRES) bound to different cellular partners. Here we report an atomic model of free full-length hepatitis C virus (IRES) refined by selection against small-angle X-ray scattering data that incorporates the known structures of different fragments. We found that an ensemble of conformers reproduces small-angle X-ray scattering data better than a single structure suggesting in combination with molecular dynamics simulations that the hepatitis C virus (IRES) is an articulated molecule made of rigid parts that move relative to each other. Principal component analysis on an ensemble of physically accessible conformers of hepatitis C virus (IRES) revealed dominant collective motions in the molecule, which may underlie the conformational changes occurring in the (IRES) molecule upon formation of the initiation complex.
Type de document :
Article dans une revue
Nature Communications, Nature Publishing Group, 2013, 4, pp.1612. 〈10.1038/ncomms2611〉
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Soumis le : lundi 18 décembre 2017 - 10:22:56
Dernière modification le : jeudi 11 janvier 2018 - 06:26:04




Julien Perard, Cedric Leyrat, Florence Baudin, Emmanuel Drouet, Marc Jamin. Structure of the full-length HCV IRES in solution. Nature Communications, Nature Publishing Group, 2013, 4, pp.1612. 〈10.1038/ncomms2611〉. 〈hal-01666137〉



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