Structure and function of the Zika virus full-length NS5 protein

Baoyu Zhao; Guanghui Yi; Fenglei Du; Yin-Chih Chuang; Robert C. Vaughan; Banumathi Sankaran; C. Cheng Kao; Pingwei Li

doi:10.1038/ncomms14762

Nature Communications (Mar 2017)

Structure and function of the Zika virus full-length NS5 protein

Baoyu Zhao,
Guanghui Yi,
Fenglei Du,
Yin-Chih Chuang,
Robert C. Vaughan,
Banumathi Sankaran,
C. Cheng Kao,
Pingwei Li

Affiliations

Baoyu Zhao: Department of Biochemistry and Biophysics, Texas A&M University
Guanghui Yi: Department of Molecular and Cellular Biochemistry, Indiana University
Fenglei Du: Department of Biochemistry and Biophysics, Texas A&M University
Yin-Chih Chuang: Department of Molecular and Cellular Biochemistry, Indiana University
Robert C. Vaughan: Department of Molecular and Cellular Biochemistry, Indiana University
Banumathi Sankaran: Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology
C. Cheng Kao: Department of Molecular and Cellular Biochemistry, Indiana University
Pingwei Li: Department of Biochemistry and Biophysics, Texas A&M University

DOI: https://doi.org/10.1038/ncomms14762
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 9

Abstract

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Zika virus infection can cause human birth defects and Guillain-Barré syndrome. Here the authors present the structures of the full-length nonstructural protein 5 and its RNA-dependent RNA polymerase domain of Zika virus, which are targets for inhibitors of virus replication.

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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