PT  - JOURNAL ARTICLE
AU  - Yin, Wanchao
AU  - Mao, Chunyou
AU  - Luan, Xiaodong
AU  - Shen, Dan-Dan
AU  - Shen, Qingya
AU  - Su, Haixia
AU  - Wang, Xiaoxi
AU  - Zhou, Fulai
AU  - Zhao, Wenfeng
AU  - Gao, Minqi
AU  - Chang, Shenghai
AU  - Xie, Yuan-Chao
AU  - Tian, Guanghui
AU  - Jiang, He-Wei
AU  - Tao, Sheng-Ce
AU  - Shen, Jingshan
AU  - Jiang, Yi
AU  - Jiang, Hualiang
AU  - Xu, Yechun
AU  - Zhang, Shuyang
AU  - Zhang, Yan
AU  - Xu, H. Eric
TI  - Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir
AID  - 10.1101/2020.04.08.032763
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.04.08.032763
4099  - http://biorxiv.org/content/early/2020/04/10/2020.04.08.032763.short
4100  - http://biorxiv.org/content/early/2020/04/10/2020.04.08.032763.full
AB  - The pandemic of Corona Virus Disease 2019 (COVID-19) caused by SARS-CoV-2 has become a global crisis. The replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp), a direct target of the antiviral drug, Remdesivir. Here we report the structure of the SARS-CoV-2 RdRp either in the apo form or in complex with a 50-base template-primer RNA and Remdesivir at a resolution range of 2.5-2.8 Å. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp where Remdesivir is incorporated into the first replicated base pair and terminates the chain elongation. Our structures provide critical insights into the working mechanism of viral RNA replication and a rational template for drug design to combat the viral infection.Competing Interest StatementThe authors have declared no competing interest.