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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
Science, 05/2020, Letnik: 368, Številka: 6492Journal Article
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.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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Povezave do osebnih bibliografij avtorjev | Povezave do podatkov o raziskovalcih v sistemu SICRIS |
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Vir: Osebne bibliografije
in: SICRIS
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