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Premium Crystal structure of full‐length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5
Upadhyay Anup K.,
Cyr Matthew,
Longenecker Kenton,
Tripathi Rakesh,
Sun Chaohong,
Kempf Dale J.
Publication year2017
Publication title
acta crystallographica section f
Resource typeJournals
PublisherInternational Union of Crystallography
The rapid spread of the recent Zika virus (ZIKV) epidemic across various countries in the American continent poses a major health hazard for the unborn fetuses of pregnant women. To date, there is no effective medical intervention. The nonstructural protein 5 of Zika virus (ZIKV‐NS5) is critical for ZIKV replication through the 5′‐RNA capping and RNA polymerase activities present in its N‐terminal methyltransferase (MTase) and C‐terminal RNA‐dependent RNA polymerase (RdRp) domains, respectively. The crystal structure of the full‐length ZIKV‐NS5 protein has been determined at 3.05 Å resolution from a crystal belonging to space group P 2 1 2 1 2 and containing two protein molecules in the asymmetric unit. The structure is similar to that reported for the NS5 protein from Japanese encephalitis virus and suggests opportunities for structure‐based drug design targeting either its MTase or RdRp domain.
Subject(s)biology , gene , genetics , polymerase , rna , rna polymerase , subgenomic mrna , virology , virus , zika virus
Keyword(s) Zika virus , NS5 , nonstructural protein 5
SCImago Journal Rank0.572

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