Article: Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
Biochemistry. 2020 June 24, v. 59, no. 28
2020
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 polymerase, helicase, and main protease, are well conserved ...
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 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. |
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Keywords | Coronavirus infections ; Orthocoronavirinae ; RNA ; RNA-directed RNA polymerase ; amino acids ; antiviral agents ; genome ; proteinases ; therapeutics ; viral nonstructural proteins ; viruses |
Language | English |
Dates of publication | 2020-0624 |
Size | p. 2608-2615. |
Publishing place | American Chemical Society |
Document type | Article |
Note | NAL-light |
ZDB-ID | 1108-3 |
ISSN | 1520-4995 ; 0006-2960 |
ISSN (online) | 1520-4995 |
ISSN | 0006-2960 |
DOI | 10.1021/acs.biochem.0c00309 |
Database | NAL-Catalogue (AGRICOLA) |
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