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dc.contributor.authorGao, Yan et al.
dc.date.accessioned2020-04-16T18:32:32Z
dc.date.available2020-04-16T18:32:32Z
dc.date.issued2020-04-10
dc.identifier.urihttps://doi.org/10.1126/science.abb7498en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12663/1048
dc.description.abstractA 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.en_US
dc.languageEnglishen_US
dc.subjectCOVID-19en_US
dc.subjectCoronavirusen_US
dc.subjectInfectious Diseasesen_US
dc.subjectDNA-Directed RNA Polymerasesen_US
dc.titleStructure of the RNA-dependent RNA polymerase from COVID-19 virusen_US
eihealth.countryOthersen_US
eihealth.categoryVirus: natural history, transmission and diagnosticsen_US
eihealth.categoryCandidate therapeutics RDen_US
eihealth.categoryCandidate vaccines RDen_US
eihealth.typePublished Articleen_US
eihealth.maincategorySave Lives / Salvar Vidasen_US
dc.relation.ispartofjournalScienceen_US


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