ArticleJournal of virology2008
Structure of the main protease from a global infectious human coronavirus, HCoV-HKU1.
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 56 papers.
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Who cites it
56 citing papers in PubMed.
- Disulfide bond formation between Cys22 and Cys44 in SARS-CoV-2 main protease.Bioorganic & medicinal chemistry letters · 2026Article
- Identification of Potent, Broad-Spectrum Coronavirus Main Protease Inhibitors for Pandemic Preparedness.Journal of medicinal chemistry · 2024Article
- A Tale of Two Proteases: MPharmaceuticals (Basel, Switzerland) · 2023Review
- A comprehensive survey of coronaviral main protease active site diversity in 3D: Identifying and analyzing drug discovery targets in search of broad specificity inhibitors for the next coronavirus pandemic.bioRxiv : the preprint server for biology · 2023Article
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.Nature communications · 2022Article
- The SARS-CoV-2 main protease (MMedComm · 2022Review
- Proteolytic Processing of the Coronavirus Replicase Nonstructural Protein 14 Exonuclease Is Not Required for Virus Replication but Alters RNA Synthesis and Viral Fitness.Journal of virology · 2022Article
- Dimerization Tendency of 3CLpros of Human Coronaviruses Based on the X-ray Crystal Structure of the Catalytic Domain of SARS-CoV-2 3CLpro.International journal of molecular sciences · 2022Article
- Repurposing dyphylline as a pan-coronavirus antiviral therapy.Future medicinal chemistry · 2022Article
- The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals.Viruses · 2022Article
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- COVID-19: inflammatory responses, structure-based drug design and potential therapeutics.Molecular diversity · 2022Review
- Review on development of potential inhibitors of SARS-CoV-2 main protease (MFuture journal of pharmaceutical sciences · 2022Review
- Characterization of the non-covalent interaction between the PF-07321332 inhibitor and the SARS-CoV-2 main protease.Journal of molecular graphics & modelling · 2022Article
- Structure-Function Characteristics of SARS-CoV-2 Proteases and Their Potential Inhibitors from Microbial Sources.Microorganisms · 2021Review
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.bioRxiv : the preprint server for biology · 2021Article
- Crystal structures of human coronavirus NL63 main protease at different pH values.Acta crystallographica. Section F, Structural biology communications · 2021Article
- What coronavirus 3C-like protease tells us: From structure, substrate selectivity, to inhibitor design.Medicinal research reviews · 2021Review
- The missing link: covalent linkages in structural models.Acta crystallographica. Section D, Structural biology · 2021Article
- Boceprevir, Calpain Inhibitors II and XII, and GC-376 Have Broad-Spectrum Antiviral Activity against Coronaviruses.ACS infectious diseases · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The newly emergent human coronavirus HKU1 (HCoV-HKU1) was first identified in Hong Kong in 2005. Infection by HCoV-HKU1 occurs worldwide and causes syndromes such as the common cold, bronchitis, and pneumonia. The CoV main protease (M(pro)), which is a key enzyme in viral replication via the proteolytic processing of the replicase polyproteins, has been recognized as an attractive target for rational drug design. In this study, we report the structure of HCoV-HKU1 M(pro) in complex with a Michael acceptor, inhibitor N3. The structure of HCoV-HKU1 provides a high-quality model for group 2A CoVs, which are distinct from group 2B CoVs such as severe acute respiratory syndrome CoV. The structure, together with activity assays, supports the relative conservation at the P1 position that was discovered by sequencing the HCoV-HKU1 genome. Combined with structural data from other CoV M(pro)s, the HCoV-HKU1 M(pro) structure reported here provides insights into both substrate preference and the design of antivirals targeting CoVs.
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