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Crystal structure of full‐length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5
Author(s) -
Upadhyay Anup K.,
Cyr Matthew,
Longenecker Kenton,
Tripathi Rakesh,
Sun Chaohong,
Kempf Dale J.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17001601
Subject(s) - zika virus , rna polymerase , virology , rna , virus , polymerase , biology , subgenomic mrna , genetics , gene
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.

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