Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
Crystals, Peptides and proteins, Genetics, Monomers, Protein structure, COVID-19
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 polymerase, 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 observed 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 a potential therapeutic target.
Frick, D. N., Virdi, R. S., Vuksanovic, N., Dahal, N., & Silvaggi, N. R. (2020). Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3. Biochemistry, 59(28), 2608–2615. https://doi.org/10.1021/acs.biochem.0c00309