Please use this identifier to cite or link to this item: https://covid-19.conacyt.mx/jspui/handle/1000/2425
Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose
David Frick.
Rajdeep S Virdi.
Nemanja Vuksanovic.
Narayan Dahal.
Nicholas R Silvaggi.
Acceso Abierto
Atribución-NoComercial-SinDerivadas
10.1101/2020.03.31.014639
The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymers, helicase and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the most novel proteins encoded by SARS-CoV-2, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those seen in other coronaviruses, the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses, and potential therapeutic target.
www.biorxiv.org
2020
Artículo
https://www.biorxiv.org/content/10.1101/2020.03.31.014639v3.full.pdf
Inglés
VIRUS RESPIRATORIOS
Appears in Collections:Artículos científicos

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