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Crystal structure of full‐length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5

Crystal structure of full‐length Zika virus NS5 protein reveals a conformation similar to... 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 P21212 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystal structure of full‐length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5

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References (50)

Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17001601
pmid
28291746
Publisher site
See Article on Publisher Site

Abstract

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 P21212 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.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ;

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