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bioRxiv · 10.1101/2020.03.31.014639

Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose

Frick, D.·Virdi, R. S.·Vuksanovic, N.·Dahal, N.·Silvaggi, N. R.
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Abstract

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 proteins encoded by SARS-CoV-2 that is most different, 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, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses, and potential therapeutic target.

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Frick, D., Virdi, R. S., Vuksanovic, N., Dahal, N., Silvaggi, N. R.. 2020-04-02. Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose. https://doi.org/10.1101/2020.03.31.014639

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