Title : The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature.

Pub. Date : 2022 May 27

PMID : 35622909






2 Functional Relationships(s)
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1 The nonstructural protein 3 (NSP3) macrodomain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (Mac1) removes adenosine diphosphate (ADP) ribosylation posttranslational modifications, playing a key role in the immune evasion capabilities of the virus responsible for the coronavirus disease 2019 pandemic. Adenosine Diphosphate ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2
2 Here, we determined neutron and x-ray crystal structures of the SARS-CoV-2 NSP3 macrodomain using multiple crystal forms, temperatures, and pHs, across the apo and ADP-ribose-bound states. Adenosine Diphosphate ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2