ArticleScientific reports2016
Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
- Inhibitor-induced dimerization mediates lufotrelvir resistance in mutants of SARS-CoV-2 3C-like protease.Protein science : a publication of the Protein Society · 2025Article
- Strategy to overcome a nirmatrelvir resistance mechanism in the SARS-CoV-2 nsp5 protease.Science advances · 2025Article
- The N-terminal peptide of the main protease of SARS-CoV-2, targeting dimer interface, inhibits its proteolytic activity.BMB reports · 2023Article
- Lessons Learnt from COVID-19: Computational Strategies for Facing Present and Future Pandemics.International journal of molecular sciences · 2023Review
- Nirmatrelvir-resistant SARS-CoV-2 variants with high fitness in an infectious cell culture system.Science advances · 2022Article
- A new inactive conformation of SARS-CoV-2 main protease.Acta crystallographica. Section D, Structural biology · 2022Article
- Proposition of a new allosteric binding site for potential SARS-CoV-2 3CL protease inhibitors by utilizing molecular dynamics simulations and ensemble docking.Journal of biomolecular structure & dynamics · 2022Article
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.bioRxiv : the preprint server for biology · 2021Article
- Flavonoids in Ampelopsis grossedentata as covalent inhibitors of SARS-CoV-2 3CLInternational journal of biological macromolecules · 2021Article
- CScientific reports · 2021Article
- Virtual high throughput screening: Potential inhibitors for SARS-CoV-2 PLEuropean journal of pharmacology · 2021Article
- Discovery of potential multi-target-directed ligands by targeting host-specific SARS-CoV-2 structurally conserved main protease.Journal of biomolecular structure & dynamics · 2021Article
- Impact of Early Pandemic Stage Mutations on Molecular Dynamics of SARS-CoV-2 MJournal of chemical information and modeling · 2020Article
- Discovery of Potential Flavonoid Inhibitors Against COVID-19 3CL Proteinase Based on Virtual Screening Strategy.Frontiers in molecular biosciences · 2020Article
- Structurally- and dynamically-driven allostery of the chymotrypsin-like proteases of SARS, Dengue and Zika viruses.Progress in biophysics and molecular biology · 2019Review
- Utilization of one novel deep-sea microbial protease sin3406-1 in the preparation of ethyl (S)-3-hydroxybutyrate through kinetic resolution.World journal of microbiology & biotechnology · 2018Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SARS 3C-like proteinase (SARS-3CLpro), which is the main proteinase of the SARS coronavirus, is essential to the virus life cycle. This enzyme has been shown to be active as a dimer in which only one protomer is active. However, it remains unknown how the dimer structure maintains an active monomer conformation. It has been observed that the Ser139-Leu141 loop forms a short 3(10)-helix that disrupts the catalytic machinery in the inactive monomer structure. We have tried to disrupt this helical conformation by mutating L141 to T in the stable inactive monomer G11A/R298A/Q299A. The resulting tetra-mutant G11A/L141T/R298A/Q299A is indeed enzymatically active as a monomer. Molecular dynamics simulations revealed that the L141T mutation disrupts the 3(10)-helix and helps to stabilize the active conformation. The coil-3(10)-helix conformational transition of the Ser139-Leu141 loop serves as an enzyme activity switch. Our study therefore indicates that the dimer structure can stabilize the active conformation but is not a required structure in the evolution of the active enzyme, which can also arise through simple mutations.
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