ArticleBiochemistry2010
Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 58 citations in OpenAlex.
- The C117D oxidation mimic reveals the monomeric structure of SARS-CoV-2 main protease.Protein science : a publication of the Protein Society · 2026Article
- Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Science advances · 2026Article
- 3-chymotrypsin-like protease in SARS-CoV-2.Bioscience reports · 2024Review
- SARS-CoV-2 MNature communications · 2024Article
- The SARS-CoV-2 MACS synthetic biology · 2024Article
- Multiple redox switches of the SARS-CoV-2 main protease in vitro provide opportunities for drug design.Nature communications · 2024Article
- The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease.Nature communications · 2023Article
- The SARS-CoV-2 main protease (MMedComm · 2022Review
- Key dimer interface residues impact the catalytic activity of 3CLpro, the main protease of SARS-CoV-2.The Journal of biological chemistry · 2022Article
- Main protease mutants of SARS-CoV-2 variants remain susceptible to nirmatrelvir.Bioorganic & medicinal chemistry letters · 2022Article
- Pro108Ser mutation of SARS-CoV-2 3CLScientific reports · 2022Article
- Maturation of the SARS-CoV-2 virus is regulated by dimerization of its main protease.Computational and structural biotechnology journal · 2022Article
- A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022Article
- Structural and functional significance of the amino acid differences ValInternational journal of biological macromolecules · 2021Article
- Allosteric Regulation of 3CL Protease of SARS-CoV-2 and SARS-CoV Observed in the Crystal Structure Ensemble.Journal of molecular biology · 2021Article
- Structure-Function Characteristics of SARS-CoV-2 Proteases and Their Potential Inhibitors from Microbial Sources.Microorganisms · 2021Review
- Natural Polyphenols Inhibit the Dimerization of the SARS-CoV-2 Main Protease: The Case of Fortunellin and Its Structural Analogs.Molecules (Basel, Switzerland) · 2021Article
- Comparative protein structure network analysis on 3CLProteins · 2021Article
- Protein structural heterogeneity: A hypothesis for the basis of proteolytic recognition by the main protease of SARS-CoV and SARS-CoV-2.Biochimie · 2021Article
- Catalytic Dyad Residues His41 and Cys145 Impact the Catalytic Activity and Overall Conformational Fold of the Main SARS-CoV-2 Protease 3-Chymotrypsin-Like Protease.Frontiers in chemistry · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Coronaviruses are responsible for a significant proportion of annual respiratory and enteric infections in humans and other mammals. The most prominent of these viruses is the severe acute respiratory syndrome coronavirus (SARS-CoV) which causes acute respiratory and gastrointestinal infection in humans. The coronavirus main protease, 3CL(pro), is a key target for broad-spectrum antiviral development because of its critical role in viral maturation and high degree of structural conservation among coronaviruses. Dimerization is an indispensable requirement for the function of SARS 3CL(pro) and is regulated through mechanisms involving both direct and long-range interactions in the enzyme. While many of the binding interactions at the dimerization interface have been extensively studied, those that are important for long-range control are not well-understood. Characterization of these dimerization mechanisms is important for the structure-based design of new treatments targeting coronavirus-based infections. Here we report that Asn28, a residue 11 A from the closest residue in the opposing monomer, is essential for the enzymatic activity and dimerization of SARS 3CL(pro). Mutation of this residue to alanine almost completely inactivates the enzyme and results in a 19.2-fold decrease in the dimerization K(d). The crystallographic structure of the N28A mutant determined at 2.35 A resolution reveals the critical role of Asn28 in maintaining the structural integrity of the active site and in orienting key residues involved in binding at the dimer interface and substrate catalysis. These findings provide deeper insight into complex mechanisms regulating the activity and dimerization of SARS 3CL(pro).
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