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

doi:10.1126/science.abb7498

GSTDTAP > 气候变化

DOI	10.1126/science.abb7498
	Structure of the RNA-dependent RNA polymerase from COVID-19 virus
	Yan Gao; Liming Yan; Yucen Huang; Fengjiang Liu; Yao Zhao; Lin Cao; Tao Wang; Qianqian Sun; Zhenhua Ming; Lianqi Zhang; Ji Ge; Litao Zheng; Ying Zhang; Haofeng Wang; Yan Zhu; Chen Zhu; Tianyu Hu; Tian Hua; Bing Zhang; Xiuna Yang; Jun Li; Haitao Yang; Zhijie Liu; Wenqing Xu; Luke W. Guddat; Quan Wang; Zhiyong Lou; Zihe Rao
	2020-05-15
发表期刊	Science
出版年	2020
英文摘要	Many in the scientific community have mobilized to understand the virus that is causing the global coronavirus disease 2019 (COVID-19) pandemic. Gao et al. focused on a complex that plays a key role in the replication and transcription cycle of the virus. They used cryo–electron microscopy to determine a 2.9-angstrom-resolution structure of the RNA-dependent RNA polymerase nsp12, which catalyzes the synthesis of viral RNA, in complex with two cofactors, nsp7 and nsp8. nsp12 is a target for nucleotide analog antiviral inhibitors such as remdesivir, and the structure may provide a basis for designing new antiviral therapeutics. Science , this issue p. [779][1] 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. [1]: /lookup/doi/10.1126/science.abb7498
领域	气候变化 ; 资源环境
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文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/267724
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Yan Gao,Liming Yan,Yucen Huang,et al. Structure of the RNA-dependent RNA polymerase from COVID-19 virus[J]. Science,2020.
APA	Yan Gao.,Liming Yan.,Yucen Huang.,Fengjiang Liu.,Yao Zhao.,...&Zihe Rao.(2020).Structure of the RNA-dependent RNA polymerase from COVID-19 virus.Science.
MLA	Yan Gao,et al."Structure of the RNA-dependent RNA polymerase from COVID-19 virus".Science (2020).