Background: Coronavirus disease 2019 is caused by exposure to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It was reported that Zn 2+ is an inhibitor of severe acute respiratory syndrome coronavirus (SARS-CoV). We hypothesize that the same applies to the newly discovered SARS-CoV-2. Material & methods: We compared the structure of RNA-dependent RNA polymerase between SARS-CoV and SARS-CoV-2. The RdRp’s binding to Zn 2+ was studied by metal ion-binding site prediction and docking server. Results: Several regions containing key residues were detected. The functional aspartic acid residues RdRp, 618D, 760D and 761D were among the predicted Zn 2+ -binding residues. Conclusion: The most probable mechanism of inhibition of RdRp by Zn 2+ is binding to the active aspartic acid triad while other binding sites can further destabilize the enzyme or interfere with the fidelity-check mechanism. Tweetable abstract The most probable mechanism of inhibition of RNA polymerase by Zn 2+ is binding to the active aspartic acid triad while other binding sites can further destabilize the enzyme or interfere with the fidelity-check mechanism. #Zinc #SARS_CoV_2 #COVID_19.
【저자키워드】 COVID-19, SARS-CoV-2, Zinc, bioinformatics, in silico, RNA-dependent RNA polymerase, 【초록키워드】 Coronavirus disease 2019, coronavirus, SARS-CoV, docking, binding site, Region, RdRP, RNA polymerase, inhibitor, mechanism, binding, acute respiratory syndrome, Abstract, enzyme, residue, residues, material, predicted, caused, reported, functional, interfere, 【제목키워드】 coronavirus, Analysis, acute respiratory syndrome, approach,