Structural Basis of the Potential Binding Mechanism of Remdesivir to SARS-CoV‑2 RNA-Dependent RNA Polymerase

• Published in: The journal of physical chemistry. B Vol. 124; no. 32; pp. 6955 - 6962
• Main Authors: Zhang, Leili, Zhou, Ruhong
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 13.08.2020
• Subjects: Adenosine Monophosphate - analogs & derivatives; Adenosine Monophosphate - chemistry; Adenosine Monophosphate - metabolism; Adenosine Triphosphate - chemistry; Adenosine Triphosphate - metabolism; Alanine - analogs & derivatives; Alanine - chemistry; Alanine - metabolism; Amino Acid Sequence; Antiviral Agents - chemistry; Antiviral Agents - metabolism; B: Biophysics; Physical Chemistry of Biological Systems and Biomolecules; Betacoronavirus - enzymology; Binding Sites; Coronavirus RNA-Dependent RNA Polymerase; COVID-19 infection; drug resistance; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - metabolism; Food and Drug Administration; Gibbs free energy; hydrogen; Hydrogen Bonding; molecular dynamics; Molecular Dynamics Simulation; pandemic; Protein Binding; RNA; RNA replication; RNA-Dependent RNA Polymerase - antagonists & inhibitors; RNA-Dependent RNA Polymerase - chemistry; RNA-Dependent RNA Polymerase - metabolism; RNA-directed RNA polymerase; SARS-CoV-2; sequence analysis; Severe acute respiratory syndrome coronavirus 2; Thermodynamics; Viral Nonstructural Proteins - antagonists & inhibitors; Viral Nonstructural Proteins - chemistry; Viral Nonstructural Proteins - metabolism; viruses

Starting from late 2019, the coronavirus disease 2019 (COVID-19) has emerged as a once-in-a-century pandemic with deadly consequences, which urgently calls for new treatments, cures, and supporting apparatuses. Recently, because of its positive results in clinical trials, remdesivir was approved by...