ArticleChemMedChem2017
An Improved Model of the Trypanosoma brucei CTP Synthetase Glutaminase Domain-Acivicin Complex.
Article in ChemMedChem, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Targeting ALDH7A1 with covalent inhibitors reveals new chemical space for prostate cancer therapy.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Filamentation of hCTPS1 with CTP.Cell & bioscience · 2025Article
- GTP-Dependent Regulation of CTP Synthase: Evolving Insights into Allosteric Activation and NHBiomolecules · 2022Review
- Structural basis for isoform-specific inhibition of human CTPS1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Glutamine Analogues Impair Cell Proliferation, the Intracellular Cycle and Metacyclogenesis inMolecules (Basel, Switzerland) · 2020Article
- An assessment of three human methylenetetrahydrofolate dehydrogenase/cyclohydrolase-ligand complexes following further refinement.Acta crystallographica. Section F, Structural biology communications · 2019Article
- An Improved Model of the Trypanosoma brucei CTP Synthetase Glutaminase Domain-Acivicin Complex.ChemMedChem · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The natural product acivicin inhibits the glutaminase activity of cytidine triphosphate (CTP) synthetase and is a potent lead compound for drug discovery in the area of neglected tropical diseases, specifically trypanosomaisis. A 2.1-Å-resolution crystal structure of the acivicin adduct with the glutaminase domain from Trypanosoma brucei CTP synthetase has been deposited in the RCSB Protein Data Bank (PDB) and provides a template for structure-based approaches to design new inhibitors. However, our assessment of that data identified deficiencies in the model. We now report an improved and corrected inhibitor structure with changes to the chirality at one position, the orientation and covalent structure of the isoxazoline moiety, and the location of a chloride ion in an oxyanion binding site that is exploited during catalysis. The model is now in agreement with established chemical principles and allows an accurate description of molecular recognition of the ligand and the mode of binding in a potentially valuable drug target.
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Registered trials
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.