ArticlePLoS neglected tropical diseases2011
Crystal structures of T. b. rhodesiense adenosine kinase complexed with inhibitor and activator: implications for catalysis and hyperactivation.
Article in PLoS neglected tropical diseases, 2011. 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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12 citing papers in PubMed, 27 citations in OpenAlex.
- Protozoan Neglected Tropical Diseases (NTDs) Target Inhibition of Alkaloids fromPharmaceuticals (Basel, Switzerland) · 2025Article
- A monomer-dimer switch modulates the activity of plant adenosine kinase.Journal of experimental botany · 2025Article
- Laboratory Selection of Trypanosomatid Pathogens for Drug Resistance.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Evolution and Functional Divergence of theFrontiers in plant science · 2020Article
- A Novel Adenosine Kinase fromInternational journal of molecular sciences · 2019Article
- Adenosine Kinase couples sensing of cellular potassium depletion to purine metabolism.Scientific reports · 2018Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- Molecular Shape Analysis-Guided Virtual Screening Platform for Adenosine Kinase Inhibitors.Bioinformatics and biology insights · 2016Article
- Structures of adenosine kinase from Trypanosoma brucei brucei.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Adenosine kinase: exploitation for therapeutic gain.Pharmacological reviews · 2013Review
- Computational elucidation of structural basis for ligand binding with Leishmania donovani adenosine kinase.BioMed research international · 2013Article
- In-silico investigation of antitrypanosomal phytochemicals from Nigerian medicinal plants.PLoS neglected tropical diseases · 2012Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe essential purine salvage pathway of Trypanosoma brucei bears interesting catalytic enzymes for chemotherapeutic intervention of Human African Trypanosomiasis. Unlike mammalian cells, trypanosomes lack de novo purine synthesis and completely rely on salvage from their hosts. One of the key enzymes is adenosine kinase which catalyzes the phosphorylation of ingested adenosine to form adenosine monophosphate (AMP) utilizing adenosine triphosphate (ATP) as the preferred phosphoryl donor. METHODS AND
findingsHere, we present the first structures of Trypanosoma brucei rhodesiense adenosine kinase (TbrAK): the structure of TbrAK in complex with the bisubstrate inhibitor P(1),P(5)-di(adenosine-5')-pentaphosphate (AP5A) at 1.55 Å, and TbrAK complexed with the recently discovered activator 4-[5-(4-phenoxyphenyl)-2H-pyrazol-3-yl]morpholine (compound 1) at 2.8 Å resolution.
conclusionsThe structural details and their comparison give new insights into substrate and activator binding to TbrAK at the molecular level. Further structure-activity relationship analyses of a series of derivatives of compound 1 support the observed binding mode of the activator and provide a possible mechanism of action with respect to their activating effect towards TbrAK.
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