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10.1021/acsinfecdis.0c00441

http://scihub22266oqcxt.onion/10.1021/acsinfecdis.0c00441
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32946224!ä!32946224

suck abstract from ncbi


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pmid32946224      ACS+Infect+Dis 2020 ; 6 (11): 2970-2978
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  • Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain #MMPMID32946224
  • Lin MH; Chang SC; Chiu YC; Jiang BC; Wu TH; Hsu CH
  • ACS Infect Dis 2020[Nov]; 6 (11): 2970-2978 PMID32946224show ga
  • The pandemic outbreak of a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has threatened the global public health and economy since late December 2019. SARS-CoV-2 encodes the conserved macro domain within nonstructural protein 3, which may reverse cellular ADP-ribosylation and potentially cut the signal of a viral infection in the cell. Herein, we report that the SARS-CoV-2 macro domain was examined as a poly-ADP-ribose (ADPR) binding module and possessed mono-ADPR cleavage enzyme activity. After confirming the ADPR binding ability via a biophysical approach, the X-ray crystal structure of the SARS-CoV-2 macro domain was determined and structurally compared with those of other viruses. This study provides structural, biophysical, and biochemical bases to further evaluate the role of the SARS-CoV-2 macro domain in the host response via ADP-ribose binding but also as a potential target for drug design against COVID-19.
  • |Adenosine Diphosphate Ribose/metabolism[MESH]
  • |Antiviral Agents/pharmacology[MESH]
  • |Betacoronavirus/*metabolism[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/*virology[MESH]
  • |Drug Design[MESH]
  • |Humans[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/*virology[MESH]
  • |Protein Conformation[MESH]
  • |Protein Domains[MESH]
  • |SARS-CoV-2[MESH]


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