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Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
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Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
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Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
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Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
Journal Article

Near-atomic cryo-EM structure of the helical measles virus nucleocapsid

2015
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Overview
Measles is a highly contagious human disease. We used cryo–electron microscopy and single particle–based helical image analysis to determine the structure of the helical nucleocapsid formed by the folded domain of the measles virus nucleoprotein encapsidating an RNA at a resolution of 4.3 angstroms. The resulting pseudoatomic model of the measles virus nucleocapsid offers important insights into the mechanism of the helical polymerization of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein. The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of measles virus binds six nucleotides, whereas the respiratory syncytial virus nucleoprotein binds seven. It provides a rational basis for further analysis of measles virus replication and transcription, and reveals potential targets for drug design.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science