The structure of Zika virus NS5 reveals a conserved domain conformation
- Univ. of California, Riverside, CA (United States); Department of Biochemistry, University of California, Riverside, Riverside, California 92521, USA
- Univ. of California, Riverside, CA (United States)
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. In conclusion, 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.
- Research Organization:
- Univ. of California, Riverside, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
- Grant/Contract Number:
- AC02-05CH11231
- OSTI ID:
- 1361212
- Journal Information:
- Nature Communications, Journal Name: Nature Communications Vol. 8; ISSN 2041-1723
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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