Structural Basis of the Potential Binding Mechanism of Remdesivir to SARS-CoV-2 RNA-Dependent RNA Polymerase
Leili Zhang, Ruhong Zhou
Abstract
from remdesivir over ATP indicates an effective replacement of ATP in blocking of the RdRp preinsertion site. Key residues D618, S549, and R555 are found to be the contributors to the binding affinity of remdesivir. These findings suggest that remdesivir can potentially act as a SARS-CoV-2 RNA-chain terminator, effectively stopping its RNA replication, with key residues also identified for future lead optimization and/or drug resistance studies.
Topics & Concepts
RNA polymeraseRNA-dependent RNA polymeraseRNAPolymeraseVirologyBinding siteCoronavirusBiologyBiochemistryChemistryEnzymeCoronavirus disease 2019 (COVID-19)MedicineGeneInfectious disease (medical specialty)DiseasePathologyViral gastroenteritis research and epidemiologySARS-CoV-2 and COVID-19 ResearchViral Infections and Immunology Research