Human coronavirus OC43 3CL protease and the potential of ML188 as a broad-spectrum lead compound: Homology modelling and molecular dynamic studies
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Date
2015
Journal Title
Journal ISSN
Volume Title
Publisher
Springer Nature
Abstract
The coronavirus 3 chymotrypsin-like protease (3CLpro) is a validated target in the design of potential
anticoronavirus inhibitors. The high degree of homology within the protease’s active site and substrate conservation
supports the identification of broad spectrum lead compounds. A previous study identified the compound ML188,
also termed 16R, as an inhibitor of the Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) 3CLpro. This study
will detail the generation of a homology model of the 3CLpro of the human coronavirus OC43 and determine the
potential of 16R to form a broad-spectrum lead compound. MODELLER was used to generate a suitable
three-dimensional model of the OC43 3CLpro and the Prime module of Schrӧdinger predicted the binding
conformation and free energy of binding of 16R within the 3CLpro active site. Molecular dynamics further
confirmed ligand stability and hydrogen bonding networks.
Description
Keywords
Covid-19, Human coronavirus, Public health, Molecular dynamics, Bioinformatics
Citation
Berry, M. et al. (2015). Human coronavirus OC43 3CL protease and the potential of ML188 as a broad-spectrum lead compound: Homology modelling and molecular dynamic studies. BMC Structural Biology, 15, 8. https://doi.org/10.1186/s12900-015-0035-3