Influence of charge configuration on substrate binding to SARS-CoV-2 main protease.
Chem Commun (Camb)
; 57(43): 5314-5317, 2021 May 27.
Article
in English
| MEDLINE | ID: covidwho-1213947
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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Peptide Hydrolases
/
SARS-CoV-2
Language:
English
Journal:
Chem Commun (Camb)
Journal subject:
Chemistry
Year:
2021
Document Type:
Article
Affiliation country:
D1cc01449h
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