Journal
CHEMICAL COMMUNICATIONS
Volume 57, Issue 43, Pages 5314-5317Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc01449h
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Funding
- FICyT [FC-GRUPIN-IDI/2018/000177]
- MICINN [PGC2018-095953-B-I00]
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While computational simulations support a neutral state for the catalytic dyad of the SARS-CoV-2 main protease, a recently-reported neutron structure shows a zwitterionic form. Molecular Dynamics study reveals that the enzyme charge configuration from the neutron structure is not compatible with a catalytically-competent binding mode for peptide substrates.
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.
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