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Copyright Nature Publishing Group Mar 2017

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.

Details

Title
The structure of Zika virus NS5 reveals a conserved domain conformation
Author
Wang, Boxiao; Tan, Xiao-feng; Thurmond, Stephanie; Zhang, Zhi-min; Lin, Asher; Hai, Rong; Song, Jikui
Pages
14763
Publication year
2017
Publication date
Mar 2017
Publisher
Nature Publishing Group
e-ISSN
20411723
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1884186440
Copyright
Copyright Nature Publishing Group Mar 2017