dc.contributor.author | Gao, Yan et al. | |
dc.date.accessioned | 2020-04-16T18:32:32Z | |
dc.date.available | 2020-04-16T18:32:32Z | |
dc.date.issued | 2020-04-10 | |
dc.identifier.uri | https://doi.org/10.1126/science.abb7498 | en_US |
dc.identifier.uri | https://hdl.handle.net/20.500.12663/1048 | |
dc.description.abstract | 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. | en_US |
dc.language | English | en_US |
dc.subject | COVID-19 | en_US |
dc.subject | Coronavirus | en_US |
dc.subject | Infectious Diseases | en_US |
dc.subject | DNA-Directed RNA Polymerases | en_US |
dc.title | Structure of the RNA-dependent RNA polymerase from COVID-19 virus | en_US |
eihealth.country | Others | en_US |
eihealth.category | Virus: natural history, transmission and diagnostics | en_US |
eihealth.category | Candidate therapeutics RD | en_US |
eihealth.category | Candidate vaccines RD | en_US |
eihealth.type | Published Article | en_US |
eihealth.maincategory | Save Lives / Salvar Vidas | en_US |
dc.relation.ispartofjournal | Science | en_US |