ArticleScientific reports2018
The protein kinase CK2 catalytic domain from Plasmodium falciparum: crystal structure, tyrosine kinase activity and inhibition.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Plasmodial Kinase Inhibitors Targeting Malaria: Recent Developments.Molecules (Basel, Switzerland) · 2020Pooled it
- FIKK1, a member of the FIKK kinase family, phosphorylates VAR2CSA and regulates adhesion of Plasmodium falciparum-infected erythrocytes to the placental receptor CSA.PLoS pathogens · 2026Article
- Host kinase regulation of Plasmodium vivax dormant and replicating liver stages.PLoS neglected tropical diseases · 2026Article
- Computational screening of natural inhibitors against Plasmodium falciparum kinases: Toward novel antimalarial therapies.PloS one · 2026Article
- Comparative analysis of the kinomes of Plasmodium falciparum, Plasmodium vivax and their host Homo sapiens.BMC genomics · 2022Article
- N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum.The Biochemical journal · 2022Article
- The catalytic subunit of Plasmodium falciparum casein kinase 2 is essential for gametocytogenesis.Communications biology · 2021Article
- Review
- Crystal structure of Arabidopsis thaliana casein kinase 2 α1.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural analysis of fungal pathogenicity-related casein kinase α subunit, Cka1, in the human fungal pathogen Cryptococcus neoformans.Scientific reports · 2019Article
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8 authors.
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Abstract
Malaria causes every year over half-a-million deaths. The emergence of parasites resistant to available treatments makes the identification of new targets and their inhibitors an urgent task for the development of novel anti-malaria drugs. Protein kinase CK2 is an evolutionary-conserved eukaryotic serine/threonine protein kinase that in Plasmodium falciparum (PfCK2) has been characterized as a promising target for chemotherapeutic intervention against malaria. Here we report a crystallographic structure of the catalytic domain of PfCK2α (D179S inactive single mutant) in complex with ATP at a resolution of 3.0 Å. Compared to the human enzyme, the structure reveals a subtly altered ATP binding pocket comprising five substitutions in the vicinity of the adenine base, that together with potential allosteric sites, could be exploited to design novel inhibitors specifically targeting the Plasmodium enzyme. We provide evidence for the dual autophosphorylation of residues Thr
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