ArticleJournal of synchrotron radiation2013
Crystal structure of human CK2α at 1.06 Å resolution.
Article in Journal of synchrotron radiation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- RAGE phosphorylation by CK2 in human epithelial cell model: Modulation of connexin 43 expression.iScience · 2026Article
- Selective Inhibition of CK2: Emerging Strategies and Future Directions.Journal of medicinal chemistry · 2026Review
- Competition between electrostatic interactions and halogen bonding in the protein-ligand system: structural and thermodynamic studies of 5,6-dibromobenzotriazole-hCK2α complexes.Scientific reports · 2022Article
- Copper Modulates the Catalytic Activity of Protein Kinase CK2.Frontiers in molecular biosciences · 2022Article
- Halogen Atoms in the Protein-Ligand System. Structural and Thermodynamic Studies of the Binding of Bromobenzotriazoles by the Catalytic Subunit of Human Protein Kinase CK2.The journal of physical chemistry. B · 2021Article
- Crystal structure of Arabidopsis thaliana casein kinase 2 α1.Acta crystallographica. Section F, Structural biology communications · 2020Article
- A promiscuous kinase inhibitor delineates the conspicuous structural features of protein kinase CK2a1.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Cell-based screen identifies a new potent and highly selective CK2 inhibitor for modulation of circadian rhythms and cancer cell growth.Science advances · 2019Article
- Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration.Acta crystallographica. Section F, Structural biology communications · 2018Article
- A π-Halogen Bond of Dibenzofuranones with the Gatekeeper Phe113 in Human Protein Kinase CK2 Leads to Potent Tight Binding Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2018Article
- Structural Hypervariability of the Two Human Protein Kinase CK2 Catalytic Subunit Paralogs Revealed by Complex Structures with a Flavonol- and a Thieno[2,3-d]pyrimidine-Based Inhibitor.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Specific inhibition of CK2α from an anchor outside the active site.Chemical science · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Ser/Thr kinase CK2 consists of two catalytic subunits (CK2α) and a dimer of the regulatory subunits (CK2β), and is a ubiquitous enzyme that regulates growth, proliferation and the survival of cells. CK2 is a remarkable drug target for potentially treating a wide variety of tumours and glomerulonephritis. The purified CK2α protein was crystallized using ethylene glycol as a precipitant. The crystal structure of CK2α with 21 loci of alternative conformations, including a niacin, 19 ethylene glycols and 346 waters, was determined at 1.06 Å resolution to an Rwork of 14.0% (Rfree = 16.5%). The alternative ensemble in the internal hydrophobic core underpins the plasticity of the αD-helix responsible for the regulation of ATP/GTP binding. The clear density map indicates that a niacin molecule, contained in the Escherichia coli culture medium, binds to the ATP binding site. An ethylene glycol molecule binds in the hydrophobic pocket lateral to the αD-helix forming the rim of the active site. The other ethylene glycol molecules occupy physiologically significant sites, including the CK2β binding interface and substrate binding site, as well as the gap in the crystal packing. Together with water molecules in the active site, these structural insights should facilitate drug discovery.
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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.