%0 Journal Article %A David N. Frick %A Rajdeep S. Virdi %A Nemanja Vuksanovic %A Narayan Dahal %A Nicholas R. Silvaggi %T Molecular Basis for ADP-ribose Binding to the Macro-X Domain of SARS-CoV-2 Nsp3 %D 2020 %R 10.1101/2020.03.31.014639 %J bioRxiv %P 2020.03.31.014639 %X 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.Competing Interest StatementThe authors have declared no competing interest. %U https://www.biorxiv.org/content/biorxiv/early/2020/04/29/2020.03.31.014639.full.pdf