PropertyValue
?:abstract
  • [Image: see text] 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.
?:creator
?:doi
  • 10.1021/acs.biochem.0c00309
?:doi
?:journal
  • Biochemistry
?:license
  • no-cc
?:pdf_json_files
  • document_parses/pdf_json/9fee92c912e8d92a2bdcf67a93a9f16ebbc193a7.json
?:pmc_json_files
  • document_parses/pmc_json/PMC7341687.xml.json
?:pmcid
?:pmid
?:pmid
  • 32578982.0
?:publication_isRelatedTo_Disease
?:sha_id
?:source
  • Medline; PMC
?:title
  • Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
?:type
?:year
  • 2020-06-29

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