ArticleScientific reports2024
Discovery and binding mode of small molecule inhibitors of the apo form of human TDO2.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Chicken IDO2 and TDO2: Biochemical Characteristics and Regulatory Roles in Avian Tryptophan Metabolism and Inflammatory Response.Animals : an open access journal from MDPI · 2026Article
- Lipophilic Ligand Efficiency-Monitored Discovery of Potent, Achiral, and Bioavailable Apo-IDO1 Inhibitors.ACS medicinal chemistry letters · 2026Article
- Discovery of a Dual IDO1/TDO Inhibitor That Modulates Enzymatic Activity and IDO1/SHP-2 Signaling.Journal of medicinal chemistry · 2026Article
- Molecular Insights Into the Interaction of Tryptophan Metabolites With Tryptophan and Indoleamine 2,3-Dioxygenases: Nitric Oxide a New Effector of Tryptophan 2,3-Dioxygenase and Their Roles in Infection.International journal of tryptophan research : IJTR · 2025Article
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Authors and funding
13 authors.
Funding
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Abstract
Tryptophan-2,3-dioxygenase (TDO2) and indoleamine-2,3-dioxygenase (IDO1) are structurally distinct heme enzymes that catalyze the conversion of L-tryptophan to N-formyl-kynurenine, and play important roles in metabolism, inflammation, and tumor immune surveillance. The enzymes can adopt an inactive, heme-free (apo) state or an active, heme-containing (holo) state, with the balance between them varying dynamically according to biological conditions. Inhibitors of holo-TDO2 are known but, despite several advantages of the heme-free state as a drug target, no inhibitors of apo-TDO2 have been reported. We describe the discovery of the first apo-TDO2 binding inhibitors, to our knowledge, and their inhibition of cellular TDO2 activity at low nanomolar concentrations. The crystal structure of a potent, small molecule inhibitor bound to apo-TDO2 reveals its detailed binding interactions within the large, hydrophobic heme binding pocket of the active site.
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