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The structure of Zika virus NS5 reveals a conserved domain conformation

Author

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  • Boxiao Wang

    (University of California, Riverside)

  • Xiao-Feng Tan

    (University of California, Riverside)

  • Stephanie Thurmond

    (University of California, Riverside)

  • Zhi-Min Zhang

    (University of California, Riverside)

  • Asher Lin

    (University of California, Riverside)

  • Rong Hai

    (University of California, Riverside)

  • Jikui Song

    (University of California, Riverside)

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.

Suggested Citation

  • Boxiao Wang & Xiao-Feng Tan & Stephanie Thurmond & Zhi-Min Zhang & Asher Lin & Rong Hai & Jikui Song, 2017. "The structure of Zika virus NS5 reveals a conserved domain conformation," Nature Communications, Nature, vol. 8(1), pages 1-6, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14763
    DOI: 10.1038/ncomms14763
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