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-Structure paper
タイトル | Structure of the RNA-dependent RNA polymerase from COVID-19 virus. |
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ジャーナル・号・ページ | Science, Vol. 368, Issue 6492, Page 779-782, Year 2020 |
掲載日 | 2020年5月15日 |
著者 | 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 / |
PubMed 要旨 | 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 ...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. |
リンク | Science / PubMed:32277040 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 - 2.95 Å |
構造データ | EMDB-30127, PDB-6m71: EMDB-30178: SARS-Cov-2 RNA-dependent RNA polymerase in complex with cofactors in reduced conditions |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | VIRAL PROTEIN / COVID-19 / 2019-nCoV / SARS-CoV-2 / Virus / RdRp / nsp12 / nsp7 / nsp8 / RTC / cryo-EM / RNA polymerase / drug target / antiviral / replication transcription complex |