High-resolution structures of the SARS-CoV-2 2′- <i>O</i> -methyltransferase reveal strategies for structure-based inhibitor design
Mónica Rosas‐Lemus, G. Minasov, L. Shuvalova, Nicole L. Inniss, O. Kiryukhina, J.S. Brunzelle, K.J.F. Satchell
Abstract
GpppA-binding pocket. Bound sulfates in several of the structures suggested the location of the ribonucleic acid backbone phosphates in the ribonucleotide-binding groove. Additional nucleotide-binding sites were found on the face of the protein opposite the active site. These various sites and the conserved dimer interface could be exploited for the development of antiviral inhibitors.
Topics & Concepts
MethyltransferaseEnzymeSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)ChemistryCoronavirus disease 2019 (COVID-19)StereochemistryBiochemistryMedicineDNAInternal medicineMethylationDiseaseInfectious disease (medical specialty)RNA and protein synthesis mechanismsRNA modifications and cancerinterferon and immune responses