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About:
Structure of RNA-dependent RNA polymerase from 2019-nCoV, a major antiviral drug target
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covidontheweb.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
Structure of RNA-dependent RNA polymerase from 2019-nCoV, a major antiviral drug target
Creator
Zhu, Yan
Wang, Tao
Rao, Zihe
Yang, Haitao
Zhang, Ying
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source
BioRxiv
abstract
A novel coronavirus (2019-nCoV) 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), which catalyzes the synthesis of viral RNA, is a key component of coronaviral replication/transcription machinery and appears to be a primary target for the antiviral drug, remdesivir. Here we report the cryo-EM structure of 2019-nCoV full-length nsp12 in complex with cofactors nsp7 and nsp8 at a resolution of 2.9-Å. Additional to the conserved architecture of the polymerase core of the viral polymerase family and a nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain featured in coronaviral RdRp, nsp12 possesses a newly identified β-hairpin domain at its N-terminal. Key residues for viral replication and transcription are observed. A comparative analysis to show how remdesivir binds to this polymerase is also provided. This structure provides insight into the central component of coronaviral replication/transcription machinery and sheds light on the design of new antiviral therapeutics targeting viral RdRp. One Sentence Summary Structure of 2019-nCov RNA polymerase.
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2020-04-09
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bibo:doi
10.1101/2020.03.16.993386
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biorxiv
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4dfb8b2c6c9eaba1010c26c5ac2e15e47c6a7fbf
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https://doi.org/10.1101/2020.03.16.993386
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Structure of RNA-dependent RNA polymerase from 2019-nCoV, a major antiviral drug target
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bioRxiv
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covid:4dfb8b2c6c9eaba1010c26c5ac2e15e47c6a7fbf#body_text
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named entity 'insight'
named entity 'machinery'
named entity 'polymerase'
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