ArticleJournal of virology2008
Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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104 citing papers in PubMed.
- Identification of Potential SARS-CoV-2 Main Protease (MPro) Inhibitors Through Pharmacophore Modeling, Molecular Docking, and Molecular Dynamics Simulation Approaches.International journal of molecular sciences · 2026Article
- Statistical crystallography reveals an allosteric network in SARS-CoV-2 MCommunications biology · 2026Article
- Solution Domain Dynamics of Monomeric SARS-CoV‑2 Main Protease Revealed by Optimized NMR Residual Dipolar Coupling Measurements.ACS physical chemistry Au · 2026Article
- Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Science advances · 2026Article
- Support Vector Machine Identification of Small Molecule Binders to an Understudied Allosteric Site of SARS-CoV-2 Mpro for Next-Generation PROTAC-Based Therapeutics.Archiv der Pharmazie · 2025Article
- Inhibitor-induced dimerization mediates lufotrelvir resistance in mutants of SARS-CoV-2 3C-like protease.Protein science : a publication of the Protein Society · 2025Article
- Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir.Communications biology · 2025Article
- Strategy to overcome a nirmatrelvir resistance mechanism in the SARS-CoV-2 nsp5 protease.Science advances · 2025Article
- Identifying Exifone as a Dual-Target Agent Targeting Both SARS-CoV-2 3CL Protease and the ACE2/S-RBD Interaction Among Clinical Polyphenolic Compounds.International journal of molecular sciences · 2025Review
- Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins.Journal of biomolecular NMR · 2025Article
- Computational Insights into Acrylamide Fragment Inhibition of SARS-CoV-2 Main Protease.Current issues in molecular biology · 2024Article
- Allostery in homodimeric SARS-CoV-2 main protease.Communications biology · 2024Article
- Identification of novel small-molecule inhibitors of SARS-CoV-2 by chemical genetics.Acta pharmaceutica Sinica. B · 2024Article
- 3-chymotrypsin-like protease in SARS-CoV-2.Bioscience reports · 2024Review
- Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.Journal of molecular biology · 2024Article
- AnHeliyon · 2024Article
- Porcine deltacoronavirus nsp5 antagonizes type I interferon signaling by cleaving IFIT3.Journal of virology · 2024Article
- The SARS-CoV-2 MACS synthetic biology · 2024Article
- Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursors.Communications biology · 2023Article
- The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease.Nature communications · 2023Article
44 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
Unlike 3C protease, the severe acute respiratory syndrome coronavirus (SARS-CoV) 3C-like protease (3CLpro) is only enzymatically active as a homodimer and its catalysis is under extensive regulation by the unique extra domain. Despite intense studies, two puzzles still remain: (i) how the dimer-monomer switch is controlled and (ii) why dimerization is absolutely required for catalysis. Here we report the monomeric crystal structure of the SARS-CoV 3CLpro mutant R298A at a resolution of 1.75 A. Detailed analysis reveals that Arg298 serves as a key component for maintaining dimerization, and consequently, its mutation will trigger a cooperative switch from a dimer to a monomer. The monomeric enzyme is irreversibly inactivated because its catalytic machinery is frozen in the collapsed state, characteristic of the formation of a short 3(10)-helix from an active-site loop. Remarkably, dimerization appears to be coupled to catalysis in 3CLpro through the use of overlapped residues for two networks, one for dimerization and another for the catalysis.
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