Selected article for: "catalytic active site and RdRp complex"
Author: Wanchao Yin; Chunyou Mao; Xiaodong Luan; Dan-Dan Shen; Qingya Shen; Haixia Su; Xiaoxi Wang; Fulai Zhou; Wenfeng Zhao; Minqi Gao; Shenghai Chang; Yuan-Chao Xie; Guanghui Tian; He-Wei Jiang; Sheng-Ce Tao; Jingshan Shen; Yi Jiang; Hualiang Jiang; Yechun Xu; Shuyang Zhang; Yan Zhang; H. Eric Xu
Title: Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir
  • Document date: 2020_4_9
    • ID: 7v7pzclb_7
    Snippet: The structure of the template-RTP RdRp complex contains one nsp12, one nsp7 and one nsp8 ( Figure 3 ). The second nsp8 in the apo structure appeared to be much more flexible in the template-RTP RdRp complex and it was not visible, therefore it was not included in the final model. In addition, the template-RTP RdRp structure contains 14 bases in the template strand, 11 bases in the primer strand, the inhibitor Remdesivir in its monophosphate form .....
    Document: The structure of the template-RTP RdRp complex contains one nsp12, one nsp7 and one nsp8 ( Figure 3 ). The second nsp8 in the apo structure appeared to be much more flexible in the template-RTP RdRp complex and it was not visible, therefore it was not included in the final model. In addition, the template-RTP RdRp structure contains 14 bases in the template strand, 11 bases in the primer strand, the inhibitor Remdesivir in its monophosphate form (RMP) (Figure 4) , as well as a pyrophosphate and two magnesium ions that may serve as catalytic ions near the active site ( Figure 5 ) (26) .

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