Structure of the tetramerization domain of measles virus phosphoprotein.

Abstract : The atomic structure of the stable tetramerization domain of the measles virus phosphoprotein shows a tight four-stranded coiled coil. Although at first sight similar to the tetramerization domain of the Sendai virus phosphoprotein, which has a hydrophilic interface, the measles virus domain has kinked helices that have a strongly hydrophobic interface and it lacks the additional N-terminal three helical bundles linking the long helices.
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Journal of Virology, American Society for Microbiology, 2013, 87 (12), pp.7166-9. 〈10.1128/JVI.00487-13〉
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Soumis le : jeudi 26 mai 2016 - 09:21:53
Dernière modification le : mardi 13 mars 2018 - 09:19:54

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Guillaume Communie, Thibaut Crépin, Damien Maurin, Malene Ringkjøbing Jensen, Martin Blackledge, et al.. Structure of the tetramerization domain of measles virus phosphoprotein.. Journal of Virology, American Society for Microbiology, 2013, 87 (12), pp.7166-9. 〈10.1128/JVI.00487-13〉. 〈hal-01321590〉

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