Structure of the RNA-dependent RNA polymerase from COVID-19 virus.
Science
; 368(6492): 779-782, 2020 05 15.
Article
in English
| MEDLINE | ID: covidwho-47347
ABSTRACT
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 ß-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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
RNA-Dependent RNA Polymerase
/
Viral Nonstructural Proteins
/
Betacoronavirus
Language:
English
Journal:
Science
Year:
2020
Document Type:
Article
Affiliation country:
Science.abb7498
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