ArticleVirology2009
Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.
Article in Virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.
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Who cites it
61 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Drug targets for corona virus: A systematic review.Indian journal of pharmacologyPooled it
- The C117D oxidation mimic reveals the monomeric structure of SARS-CoV-2 main protease.Protein science : a publication of the Protein Society · 2026Article
- Exploring covalent inhibitors of SARS-CoV-2 main protease: from peptidomimetics to novel scaffolds.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir.Communications biology · 2025Article
- Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins.Journal of biomolecular NMR · 2025Article
- Research Progress on the Structure and Function, Immune Escape Mechanism, Antiviral Drug Development Methods, and Clinical Use of SARS-CoV-2 MMolecules (Basel, Switzerland) · 2025Review
- Revealing SARS-CoV-2 MComputational and structural biotechnology journal · 2024Article
- Inhibition of the SARS-CoV-2 Non-structural Protein 5 (NSP5) Protease by Nitrosocarbonyl-Bases Small Molecules.ACS omega · 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
- Identification of compounds from natural Peruvian sources as potential inhibitors of SARS-CoV-2 Mpro mutations by virtual screening and computational simulations.F1000Research · 2024Article
- Unveiling mutation effects on the structural dynamics of the main protease from SARS-CoV-2 with hybrid simulation methods.Journal of molecular graphics & modelling · 2023Article
- SARS-CoV-2 MACS central science · 2023Article
- Stabilization of the Dimeric State of SARS-CoV-2 Main Protease by GC376 and Nirmatrelvir.International journal of molecular sciences · 2023Article
- Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor.Journal of molecular biology · 2022Article
- Functional map of SARS-CoV-2 3CL protease reveals tolerant and immutable sites.Cell host & microbe · 2022Article
- NMR Observation of Sulfhydryl Signals in SARS-CoV-2 Main Protease Aids Structural Studies.Chembiochem : a European journal of chemical biology · 2022Article
- Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domain.Communications biology · 2022Article
- Effect of pH on stability of dimer structure of the main protease of coronavirus-2.Biophysical chemistry · 2022Article
- Article
1 more citing papers are in PubMed but not listed here.
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9 authors.
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Abstract
The 3C-like protease of SARS coronavirus (SARS-CoV 3CL(pro)) is vital for SARS-CoV replication and is a promising drug target. It has been extensively proved that only the dimeric enzyme is active. Here we discovered that two adjacent mutations (Ser139_Ala and Phe140_Ala) on the dimer interface resulted in completely different crystal structures of the enzyme, demonstrating the distinct roles of these two residues in maintaining the active conformation of SARS-CoV 3CL(pro). S139A is a monomer that is structurally similar to the two reported monomers G11A and R298A. However, this mutant still retains a small fraction of dimer in solution, which might account for its remaining activity. F140A is a dimer with the most collapsed active pocket discovered so far, well-reflecting the stabilizing role of this residue. Moreover, a plausible dimerization mechanism was also deduced from structural analysis. Our work is expected to provide insight on the dimerization-function relationship of SARS-CoV 3CL(pro).
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