ArticleStructure (London, England : 1993)2022
Structure of the poxvirus decapping enzyme D9 reveals its mechanism of cap recognition and catalysis.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Exploring drug repurposing for monkeypox virus: A structural and computational approach.Journal of Taibah University Medical Sciences · 2026Article
- The strategies and advances of mRNA translation booster.Asian journal of pharmaceutical sciences · 2025Review
- Biochemical and functional characterization of orf virus decapping protein OV71.Virology journal · 2025Article
- Aptamer-based assay for high-throughput substrate profiling of RNA decapping enzymes.Nucleic acids research · 2024Article
- Mechanisms and consequences of mRNA destabilization during viral infections.Virology journal · 2024Review
- In silico identification of potential inhibitors of vital monkeypox virus proteins from FDA approved drugs.Molecular diversity · 2023Article
- Fluorescence-Based Activity Screening Assay Reveals Small Molecule Inhibitors of Vaccinia Virus mRNA Decapping Enzyme D9.ACS chemical biology · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Poxviruses encode decapping enzymes that remove the protective 5' cap from both host and viral mRNAs to commit transcripts for decay by the cellular exonuclease Xrn1. Decapping by these enzymes is critical for poxvirus pathogenicity by means of simultaneously suppressing host protein synthesis and limiting the accumulation of viral double-stranded RNA (dsRNA), a trigger for antiviral responses. Here we present a high-resolution structural view of the vaccinia virus decapping enzyme D9. This Nudix enzyme contains a domain organization different from other decapping enzymes in which a three-helix bundle is inserted into the catalytic Nudix domain. The 5' mRNA cap is positioned in a bipartite active site at the interface of the two domains. Specificity for the methylated guanosine cap is achieved by stacking between conserved aromatic residues in a manner similar to that observed in canonical cap-binding proteins VP39, eIF4E, and CBP20, and distinct from eukaryotic decapping enzyme Dcp2.
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