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《Science，5月15日，Structure of the RNA-dependent RNA polymerase from COVID-19 virus》

  • 来源专题：COVID-19科研动态监测
  • 编译者： zhangmin
  • 发布时间：2020-05-16

  • Structure of the RNA-dependent RNA polymerase from COVID-19 virus

    Yan Gao1,2,*, Liming Yan1,*, Yucen Huang1,*, Fengjiang Liu2,*, Yao Zhao2, Lin Cao3, Tao Wang1, Qianqian Sun2, Zhenhua Ming4, Lianqi Zhang1, Ji Ge1, Litao Zheng1, Ying Zhang1, Haofeng Wang2,5, Yan Zhu2, Chen Zhu2, Tianyu Hu2, Tian Hua2, Bing Zhang2, Xiuna Yang2, Jun Li2, Haitao Yang2, Zhijie Liu2, Wenqing Xu2, Luke W. Guddat6, Quan Wang2,†, Zhiyong Lou1,†, Zihe Rao1,2,3,7,†

    See all authors and affiliations

    Science 15 May 2020:

    Vol. 368, Issue 6492, pp. 779-782

    DOI: 10.1126/science.abb7498

    Abstract

    A novel coronavirus [severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is the central component of coronaviral replication and transcription machinery, and it appears to be a primary target for the antiviral drug remdesivir. We report the cryo–electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-angstrom resolution. In addition to the conserved architecture of the polymerase core of the viral polymerase family, nsp12 possesses a newly identified β-hairpin domain at its N terminus. A comparative analysis model shows how remdesivir binds to this polymerase. The structure provides a basis for the design of new antiviral therapeutics that target viral RdRp.

  • 原文来源：https://science.sciencemag.org/content/368/6492/779
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