The structure of Zika virus NS5 reveals a conserved domain conformation

Boxiao Wang; Xiao-Feng Tan; Stephanie Thurmond; Zhi-Min Zhang; Asher Lin; Rong Hai; Jikui Song

doi:10.1038/ncomms14763

Nature Communications (Mar 2017)

The structure of Zika virus NS5 reveals a conserved domain conformation

Boxiao Wang,
Xiao-Feng Tan,
Stephanie Thurmond,
Zhi-Min Zhang,
Asher Lin,
Rong Hai,
Jikui Song

Affiliations

Boxiao Wang: Department of Biochemistry, University of California, Riverside
Xiao-Feng Tan: Department of Biochemistry, University of California, Riverside
Stephanie Thurmond: Department of Plant Pathology and Microbiology, University of California, Riverside
Zhi-Min Zhang: Department of Biochemistry, University of California, Riverside
Asher Lin: Department of Biochemistry, University of California, Riverside
Rong Hai: Department of Plant Pathology and Microbiology, University of California, Riverside
Jikui Song: Department of Biochemistry, University of California, Riverside

DOI: https://doi.org/10.1038/ncomms14763
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 6

Abstract

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The recent outbreak of Zika virus is a major worldwide health concern and effective drugs are currently not available. Here the authors present the structure of Zika non-structural protein 5 and identify a potential drug-binding site, which might facilitate the development of novel antivirals.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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