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Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir.
Yin, Wanchao; Mao, Chunyou; Luan, Xiaodong; Shen, Dan-Dan; Shen, Qingya; Su, Haixia; Wang, Xiaoxi; Zhou, Fulai; Zhao, Wenfeng; Gao, Minqi; Chang, Shenghai; Xie, Yuan-Chao; Tian, Guanghui; Jiang, He-Wei; Tao, Sheng-Ce; Shen, Jingshan; Jiang, Yi; Jiang, Hualiang; Xu, Yechun; Zhang, Shuyang; Zhang, Yan; Xu, H Eric.
  • Yin W; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Mao C; Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Luan X; Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Shen DD; School of Medicine, Tsinghua University, Haidian District, Beijing 100084, China.
  • Shen Q; Department of Cardiology, Peking Union Medical College Hospital, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730, China.
  • Su H; Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China.
  • Wang X; Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Zhou F; Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Zhao W; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Gao M; University of Chinese Academy of Sciences, Beijing 100049, China.
  • Chang S; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Xie YC; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Tian G; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Jiang HW; WuxiBiortus Biosciences Co. Ltd., Jiangyin 214437, China.
  • Tao SC; Center of Cryo-Electron Microscopy, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Shen J; Center of Diagnostic Electron Microscopy, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Jiang Y; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Jiang H; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Xu Y; Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University, Shanghai 200240, China.
  • Zhang S; Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University, Shanghai 200240, China.
  • Zhang Y; The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Xu HE; University of Chinese Academy of Sciences, Beijing 100049, China.
Science ; 368(6498): 1499-1504, 2020 06 26.
Article in English | MEDLINE | ID: covidwho-154668
Preprint
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ABSTRACT
The pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a global crisis. Replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp) enzyme, a target of the antiviral drug remdesivir. Here we report the cryo-electron microscopy structure of the SARS-CoV-2 RdRp, both in the apo form at 2.8-angstrom resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5-angstrom resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation. Our structures provide insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antiviral Agents / RNA-Dependent RNA Polymerase / Adenosine Monophosphate / Viral Nonstructural Proteins / Alanine / Betacoronavirus Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abc1560

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antiviral Agents / RNA-Dependent RNA Polymerase / Adenosine Monophosphate / Viral Nonstructural Proteins / Alanine / Betacoronavirus Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abc1560