ArticleStructure (London, England : 1993)2009
Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 196 citations in OpenAlex.
- Black Sheep: Pseudokinases Bucking the Trend to Reveal Non-Catalytic Kinase Functions.IUBMB life · 2026Review
- VRK3 promotes KSHV infection by suppressing the antiviral type I interferon response.PLoS pathogens · 2026Article
- SERPINI1 functions as a tumor suppressor in glioma.Scientific reports · 2026Article
- Structure-based discovery of selective vaccinia-related kinase 1 inhibitors and fluorogenic active-site probes.The Journal of biological chemistry · 2026Article
- Emergence of Catalytic Activity in VRK3: Phosphoproteomic Insights into the Regulatory Network of a Former Pseudokinase.Proteomes · 2026Review
- Dr. Kinase: predicting the drug-resistance hotspots of protein kinases.Nucleic acids research · 2025Article
- How many kinases are druggable? A review of our current understanding.The Biochemical journal · 2023Article
- Vaccinia-related kinase 2 variants differentially affect breast cancer growth by regulating kinase activity.Oncology research · 2023Article
- Decoding Diabetes Biomarkers and Related Molecular Mechanisms by Using Machine Learning, Text Mining, and Gene Expression Analysis.International journal of environmental research and public health · 2022Article
- Dissecting the roles of Haspin and VRK1 in histone H3 phosphorylation during mitosis.Scientific reports · 2022Article
- Dysregulation of Cellular VRK1, BAF, and Innate Immune Signaling by the Vaccinia Virus B12 Pseudokinase.Journal of virology · 2022Article
- Spatiotemporal expression of regulatory kinases directs the transition from mitosis to cellular morphogenesis in Drosophila.Nature communications · 2022Article
- Computational tools and resources for pseudokinase research.Methods in enzymology · 2022Review
- Recent advances in targeting protein kinases and pseudokinases in cancer biology.Frontiers in cell and developmental biology · 2022Review
- Dynamics of protein kinases and pseudokinases by HDX-MS.Methods in enzymology · 2022Article
- Landscape of drug-resistance mutations in kinase regulatory hotspots.Briefings in bioinformatics · 2021Article
- Barrier-to-autointegration factor: a first responder for repair of nuclear ruptures.Cell cycle (Georgetown, Tex.) · 2021Review
- Dimeric Structure of the Pseudokinase IRAK3 Suggests an Allosteric Mechanism for Negative Regulation.Structure (London, England : 1993) · 2021Article
- Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix.Nature communications · 2021Article
- KinaseMD: kinase mutations and drug response database.Nucleic acids research · 2021Article
42 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases, but the structural details of kinase inactivation have remained unclear. We present the first structure of a pseudokinase, VRK3, and that of its closest active relative, VRK2. Profound changes to the active site region underlie the loss of catalytic activity, and VRK3 cannot bind ATP because of residue substitutions in the binding pocket. However, VRK3 still shares striking structural similarity with VRK2, and appears to be locked in a pseudoactive conformation. VRK3 also conserves residue interactions that are surprising in the absence of enzymatic function; these appear to play important architectural roles required for the residual functions of VRK3. Remarkably, VRK3 has an "inverted" pattern of sequence conservation: although the active site is poorly conserved, portions of the molecular surface show very high conservation, suggesting that they form key interactions that explain the evolutionary retention of VRK3.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.