ArticleAntiviral research2014
Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features.
Article in Antiviral research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.
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Who cites it
62 citing papers in PubMed, 1 synthesis or guideline pooled it.
- What Have We Learned About Middle East Respiratory Syndrome Coronavirus Emergence in Humans? A Systematic Literature Review.Vector borne and zoonotic diseases (Larchmont, N.Y.) · 2019Pooled it
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Mutational profiling of SARS-CoV-2 papain-like protease reveals requirements for function, structure, and drug escape.Nature communications · 2024Article
- Local energetic frustration conservation in protein families and superfamilies.Nature communications · 2023Article
- Screening and identification of potential MERS-CoV papain-like protease (PLpro) inhibitors; Steady-state kinetic and Molecular dynamic studies.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023Article
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- Computational studies of potential antiviral compounds from some selected Nigerian medicinal plants against SARS-CoV-2 proteins.Informatics in medicine unlocked · 2023Article
- Identification of Doxorubicin as Repurposing Inhibitory Drug for MERS-CoV PLpro.Molecules (Basel, Switzerland) · 2022Article
- Chemical screen uncovers novel structural classes of inhibitors of the papain-like protease of coronaviruses.iScience · 2022Article
- Surgical Strikes on Host Defenses: Role of the Viral Protease Activity in Innate Immune Antagonism.Pathogens (Basel, Switzerland) · 2022Review
- A Review of the Potential Effects of Melatonin in Compromised Mitochondrial Redox Activities in Elderly Patients With COVID-19.Frontiers in nutrition · 2022Review
- Destruction mechanisms of ozone over SARS-CoV-2.Scientific reports · 2021Article
- Repurposing of FDA-approved antivirals, antibiotics, anthelmintics, antioxidants, and cell protectives against SARS-CoV-2 papain-like protease.Journal of biomolecular structure & dynamics · 2021Article
- SARS-CoV-2 and other coronaviruses negatively influence mitochondrial quality control: beneficial effects of melatonin.Pharmacology & therapeutics · 2021Review
- An update on emerging therapeutics to combat COVID-19.Basic & clinical pharmacology & toxicology · 2021Review
- Role of Virally-Encoded Deubiquitinating Enzymes in Regulation of the Virus Life Cycle.International journal of molecular sciences · 2021Review
- Computational prediction of nimbanal as potential antagonist of respiratory syndrome coronavirus.Informatics in medicine unlocked · 2021Article
- The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Review
- Revisiting potential druggable targets against SARS-CoV-2 and repurposing therapeutics under preclinical study and clinical trials: A comprehensive review.Drug development research · 2020Review
- Identification of novel human USP2 inhibitor and its putative role in treatment of COVID-19 by inhibiting SARS-CoV-2 papain-like (PLpro) protease.Computational biology and chemistry · 2020Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
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Abstract
The Middle-East Respiratory Syndrome coronavirus (MERS-CoV) causes severe acute pneumonia and renal failure. The MERS-CoV papain-like protease (PL(pro)) is a potential target for the development of antiviral drugs. To facilitate these efforts, we determined the three-dimensional structure of the enzyme by X-ray crystallography. The molecule consists of a ubiquitin-like domain and a catalytic core domain. The catalytic domain displays an extended right-hand fold with a zinc ribbon and embraces a solvent-exposed substrate-binding region. The overall structure of the MERS-CoV PL(pro) is similar to that of the corresponding SARS-CoV enzyme, but the architecture of the oxyanion hole and of the S3 as well as the S5 specificity sites differ from the latter. These differences are the likely reason for reduced in vitro peptide hydrolysis and deubiquitinating activities of the MERS-CoV PL(pro), compared to the homologous enzyme from the SARS coronavirus. Introduction of a side-chain capable of oxyanion stabilization through the Leu106Trp mutation greatly enhances the in vitro catalytic activity of the MERS-CoV PL(pro). The unique features observed in the crystal structure of the MERS-CoV PL(pro) should allow the design of antivirals that would not interfere with host ubiquitin-specific proteases.
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