ArticleStructure (London, England : 1993)2013
Crystal structures of the viral protease Npro imply distinct roles for the catalytic water in catalysis.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- First Identification, Recombinant Production, and Structural Characterization of a Putative Structural Protein from the Haseki Tick Virus Polyprotein.Biomolecules · 2025Article
- Current progress on innate immune evasion mediated by NFrontiers in immunology · 2023Review
- A double deletion prevents replication of the pestivirus bovine viral diarrhea virus in the placenta of pregnant heifers.PLoS pathogens · 2021Article
- PROFICS: A bacterial selection system for directed evolution of proteases.The Journal of biological chemistry · 2021Article
- Complex Virus-Host Interactions Involved in the Regulation of Classical Swine Fever Virus Replication: A Minireview.Viruses · 2017Review
- Pestivirus Npro Directly Interacts with Interferon Regulatory Factor 3 Monomer and Dimer.Journal of virology · 2016Article
- X-ray structure of the pestivirus NS3 helicase and its conformation in solution.Journal of virology · 2015Article
- Article
- Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.Journal of virology · 2014Article
- The structure of classical swine fever virus N(pro): a novel cysteine Autoprotease and zinc-binding protein involved in subversion of type I interferon induction.PLoS pathogens · 2013Article
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Authors and funding
7 authors.
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Abstract
Npro is a key effector protein of pestiviruses such as bovine viral diarrhea virus and abolishes host cell antiviral defense mechanisms. Synthesized as the N-terminal part of the viral polyprotein, Npro releases itself via an autoproteolytic cleavage, triggering its immunological functions. However, the mechanisms of its proteolytic action and its immune escape were unclear. Here, we present the crystal structures of Npro to 1.25 Å resolution. Structures of pre- and postcleavage intermediates identify three catalytically relevant elements. The trapping of the putative catalytic water reveals its distinct roles as a base, acid, and nucleophile. The presentation of the substrate further explains the enigmatic latency of the protease, ensuring a single in cis cleavage. Additionally, we identified a zinc-free, disulfide-linked conformation of the TRASH motif, an interaction hub of immune factors. The structure opens additional opportunities in utilizing Npro as an autocleaving fusion protein and as a pharmaceutical target.
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