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- Biochemistry 2020-07;
Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
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To facilitate the comparison between SARS-CoV and SARS-CoV-2, a protein expression vector was generated that is similar to that used by Eglott et al.14 To this end, a codon-optimized open reading frame was synthesized by GenScript (Piscataway, NJ) that encodes the Mac1 domain with an N-terminal TEV-cleavage site flanked by NheI and BamHI restriction sites. | |
AbstractThe 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... More KeywordsMost Popular Services
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