Issue 43, 2021

Influence of charge configuration on substrate binding to SARS-CoV-2 main protease

Abstract

While the state-of-the-art computational simulations support the neutral state for the catalytic dyad of the SARS-CoV-2 main protease, the recently-reported neutron structure exhibits a zwitterionic form. To better compare the structural and dynamical features of the two charge configurations, we perform a Molecular Dynamics study of the dimeric enzyme in complex with a peptide substrate. The simulations show that the enzyme charge configuration from the neutron structure is not compatible with a catalytically-competent binding mode for peptide substrates.

Graphical abstract: Influence of charge configuration on substrate binding to SARS-CoV-2 main protease

Supplementary files

Article information

Article type
Communication
Submitted
17 Mar 2021
Accepted
26 Apr 2021
First published
27 Apr 2021

Chem. Commun., 2021,57, 5314-5317

Influence of charge configuration on substrate binding to SARS-CoV-2 main protease

N. Díaz and D. Suárez, Chem. Commun., 2021, 57, 5314 DOI: 10.1039/D1CC01449H

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