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10.1021/acs.biochem.0c00309

http://scihub22266oqcxt.onion/10.1021/acs.biochem.0c00309
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32578982!7341687!32578982
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suck abstract from ncbi

pmid32578982
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  • Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3 #MMPMID32578982
  • Frick DN; Virdi RS; Vuksanovic N; Dahal N; Silvaggi NR
  • Biochemistry 2020[Jul]; 59 (28): 2608-2615 PMID32578982show ga
  • 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.
  • |Adenosine Diphosphate Ribose/metabolism[MESH]
  • |Betacoronavirus/*chemistry[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/drug therapy/virology[MESH]
  • |Coronavirus Papain-Like Proteases[MESH]
  • |Coronavirus/chemistry[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Drug Delivery Systems[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/drug therapy/virology[MESH]
  • |Protein Domains[MESH]
  • |SARS-CoV-2[MESH]
  • |Thermodynamics[MESH]
  • |Viral Nonstructural Proteins/*chemistry/metabolism[MESH]


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  • suck abstract from ncbi

    2608 28.59 2020