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Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Gao Yan.
Yan Liming.
Huang Yucen.
Liu Fengjiang.
Zhao Yao.
Cao Lin.
Wang Tao.
Sun Qianqian.
Ming Zhenhua.
Zhang Lianqi.
Ge Ji.
Zheng Litao.
Zhang Ying.
Wang Haofeng.
Zhu Yan.
Zhu Chen.
Hu Tianyu.
Hua Tian.
Zhang Bing.
Yang Xiuna.
Li Jun.
Yang Haitao.
Liu Zhijie.
Xu Wenqing.
Guddat Luke W..
Wang Quan.
Lou Zhiyong.
Rao Zihe.
Acceso Abierto
Atribución-NoComercial-SinDerivadas
10.1126/science.abb7498
A novel coronavirus (COVID-19 virus) outbreak has caused a global 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/transcription machinery and appears to be a primary target for the antiviral drug, remdesivir. We report the cryo-EM structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-Å 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 targeting viral RdRp.
Science
2020
Artículo
https://science.sciencemag.org/content/sci/early/2020/04/09/science.abb7498.full.pdf
Inglés
VIRUS RESPIRATORIOS
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