The structure of Zika virus NS5 reveals a conserved domain conformation [electronic resource]

• Ngôn ngữ: eng
• Ký hiệu phân loại: 572.6 Proteins
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2017
• Mô tả vật lý: Size: Article No. 14763 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 260571
• Chủ đề: 1. 59 basic biological sciences; 2. 60 applied life sciences; 3. Drug discovery; 4. X-ray crystallography

Tóm tắt

 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 <
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  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.