The structure of Zika virus NS5 reveals a conserved domain conformation.

Abstract:

:The recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structural analysis leads to the identification of a potential drug-binding site of ZIKV NS5, which might facilitate the development of novel antivirals for ZIKV.

journal_name

Nat Commun

journal_title

Nature communications

authors

Wang B,Tan XF,Thurmond S,Zhang ZM,Lin A,Hai R,Song J

doi

10.1038/ncomms14763

subject

Has Abstract

pub_date

2017-03-27 00:00:00

pages

14763

issn

2041-1723

pii

ncomms14763

journal_volume

8

pub_type

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