ArticleJournal of molecular biology2005
Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.
Article in Journal of molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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93 citing papers in PubMed, 181 citations in OpenAlex.
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- Structure and function of SARS-CoV and SARS-CoV-2 main proteases and their inhibition: A comprehensive review.European journal of medicinal chemistry · 2023Review
- αβ,α'β'-Diepoxyketones are mechanism-based inhibitors of nucleophilic cysteine enzymes.Chemical communications (Cambridge, England) · 2023Article
- Pharmacophore Oriented MP2 Characterization of Charge Distribution for Anti-SARS-CoV-2 Inhibitor Nirmatrelvir.Journal of molecular structure · 2023Article
- Green and rapid and instrumental one-pot method for the synthesis of imidazolines having potential anti-SARS-CoV-2 main protease activity.Sustainable chemistry and pharmacy · 2023Article
- PRSC chemical biology · 2023Review
- 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
- Potential treatments of COVID-19: Drug repurposing and therapeutic interventions.Journal of pharmacological sciences · 2023Review
- Dock-able linear and homodetic di, tri, tetra and pentapeptide library from canonical amino acids: SARS-CoV-2 Mpro as a case study.Journal of pharmaceutical analysis · 2023Article
- Azapeptide activity-based probes for the SARS-CoV-2 main protease enable visualization of inhibition in infected cells.Chemical science · 2023Article
- Novel covalent and non-covalent complex-based pharmacophore models of SARS-CoV-2 main protease (MScientific reports · 2022Article
- A new inactive conformation of SARS-CoV-2 main protease.Acta crystallographica. Section D, Structural biology · 2022Article
- COVID-19: inflammatory responses, structure-based drug design and potential therapeutics.Molecular diversity · 2022Review
- Fungal Proteases as Emerging Biocatalysts to Meet the Current Challenges and Recent Developments in Biomedical Therapies: An Updated Review.Journal of fungi (Basel, Switzerland) · 2022Review
- Review on development of potential inhibitors of SARS-CoV-2 main protease (MFuture journal of pharmaceutical sciences · 2022Review
- Perspectives on SARS-CoV-2 Main Protease Inhibitors.Journal of medicinal chemistry · 2021Review
- Allosteric Regulation of 3CL Protease of SARS-CoV-2 and SARS-CoV Observed in the Crystal Structure Ensemble.Journal of molecular biology · 2021Article
- Innate immune evasion mediated by picornaviral 3C protease: Possible lessons for coronaviral 3C-like protease?Reviews in medical virology · 2021Review
- Pharmacoinformatics and molecular dynamics simulation studies reveal potential covalent and FDA-approved inhibitors of SARS-CoV-2 main protease 3CLJournal of biomolecular structure & dynamics · 2021Article
33 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The main peptidase (M(pro)) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV M(pro) by an aza-peptide epoxide (APE; k(inact)/K(i) = 1900(+/-400) M(-1) s(-1)). The crystal structures of the M(pro):APE complex in the space groups C2 and P2(1)2(1)2(1) revealed the formation of a covalent bond between the catalytic Cys145 S(gamma) atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of M(pro) in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound M(pro) in the space group C2 revealed that the "N-fingers" (N-terminal residues 1 to 7) of both protomers of M(pro) are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound M(pro) in the space group P2(1).
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