RT Journal Article
SR Electronic
T1 Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.04.08.032763
DO 10.1101/2020.04.08.032763
A1 Yin, Wanchao
A1 Mao, Chunyou
A1 Luan, Xiaodong
A1 Shen, Dan-Dan
A1 Shen, Qingya
A1 Su, Haixia
A1 Wang, Xiaoxi
A1 Zhou, Fulai
A1 Zhao, Wenfeng
A1 Gao, Minqi
A1 Chang, Shenghai
A1 Xie, Yuan-Chao
A1 Tian, Guanghui
A1 Jiang, He-Wei
A1 Tao, Sheng-Ce
A1 Shen, Jingshan
A1 Jiang, Yi
A1 Jiang, Hualiang
A1 Xu, Yechun
A1 Zhang, Shuyang
A1 Zhang, Yan
A1 Xu, H. Eric
YR 2020
UL http://biorxiv.org/content/early/2020/04/10/2020.04.08.032763.abstract
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.