Cryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses.

JOURNAL OF VIROLOGY(2012)

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摘要
Cryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical core, indicative of gene duplication. This unusual organization is common to chrysoviruses. The arrangement of many of these putative alpha-helices is conserved in the totivirus L-A capsid protein, suggesting a shared motif. Our results indicate that a 120-,subunit T=1 capsid is a conserved architecture that optimizes dsRNA replication and organization.
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关键词
protein folding,virus replication
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