Title : Allosteric Activation of SARS-CoV-2 RNA-Dependent RNA Polymerase by Remdesivir Triphosphate and Other Phosphorylated Nucleotides.

Pub. Date : 2021 Jun 29

PMID : 34154407






3 Functional Relationships(s)
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1 Our data show that adenosine and remdesivir triphosphates promote the synthesis of A-less RNAs, as does ppGpp, while amino acid substitutions at the NiRAN-RdRp interface augment activation, suggesting that ligand binding to the NiRAN catalytic site modulates RdRp activity. remdesivir ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2
2 Our data show that adenosine and remdesivir triphosphates promote the synthesis of A-less RNAs, as does ppGpp, while amino acid substitutions at the NiRAN-RdRp interface augment activation, suggesting that ligand binding to the NiRAN catalytic site modulates RdRp activity. remdesivir ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2
3 Using this assay, we demonstrate that RdRp is allosterically activated by nontemplating phosphorylated nucleotides, including naturally occurring alarmone ppGpp and synthetic remdesivir triphosphate. remdesivir ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2