ArticleProteins2006
Binding site-based classification of coronaviral papain-like proteases.
Article in Proteins, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Quinazolinone based broad-spectrum antiviral molecules: design, synthesis, in silico studies and biological evaluation.Molecular diversity · 2026Article
- Analysis of Structures of SARS-CoV-2 Papain-like Protease Bound with Ligands Unveils Structural Features for Inhibiting the Enzyme.Molecules (Basel, Switzerland) · 2025Review
- Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin.Nature communications · 2023Article
- Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin.bioRxiv : the preprint server for biology · 2023Article
- High-throughput screening of SARS-CoV-2 main and papain-like protease inhibitors.Protein & cell · 2023Article
- 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
- Dissection of amino-terminal functional domains of murine coronavirus nonstructural protein 3.Journal of virology · 2015Article
- The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor.Biological chemistry · 2014Review
- Coat protein expression strategy of oat blue dwarf virus.Virology · 2014Article
- Comparison of SARS and NL63 papain-like protease binding sites and binding site dynamics: inhibitor design implications.Journal of molecular biology · 2011Article
- Papain-like protease 1 from transmissible gastroenteritis virus: crystal structure and enzymatic activity toward viral and cellular substrates.Journal of virology · 2010Article
- Exchange of the coronavirus replicase polyprotein cleavage sites alters protease specificity and processing.Journal of virology · 2010Article
- Ubiquitin and ubiquitin-like specific proteases targeted by infectious pathogens: Emerging patterns and molecular principles.Biochimica et biophysica acta · 2008Review
- A noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease.Archives of biochemistry and biophysics · 2007Article
- Article
- Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.Journal of virology · 2007Article
- Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication.Journal of virology · 2007Article
- Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3.Journal of virology · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coronavirus replicase gene encodes one or two papain-like proteases (termed PL1pro and PL2pro) implicated in the N-terminal processing of the replicase polyprotein and thus contributing to the formation of the viral replicase complex that mediates genome replication. Using consensus fold recognition with the 3D-JURY meta-predictor followed by model building and refinement, we developed a structural model for the single PLpro present in the severe acute respiratory syndrome coronavirus (SCoV) genome, based on significant structural relationships to the catalytic core domain of HAUSP, a ubiquitin-specific protease (USP). By combining the SCoV PLpro model with comparative sequence analyses we show that all currently known coronaviral PLpros can be classified into two groups according to their binding site architectures. One group includes all PL2pros and some of the PL1pros, which are characterized by a restricted USP-like binding site. This group is designated the R-group. The remaining PL1pros from some of the coronaviruses form the other group, featuring a more open papain-like binding site, and is referred to as the O-group. This two-group, binding site-based classification is consistent with experimental data accumulated to date for the specificity of PLpro-mediated polyprotein processing and PLpro inhibition. It also provides an independent evaluation of the similarity-based annotation of PLpro-mediated cleavage sites, as well as a basis for comparison with previous groupings based on phylogenetic analyses.
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