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8W1H

Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PYN3 inhibitor

This is a non-PDB format compatible entry.
Summary for 8W1H
Entry DOI10.2210/pdb8w1h/pdb
Related8VTQ 8VUG 8W2K 9AT2
DescriptorTryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE, alpha-methyl-L-tryptophan, ... (5 entities in total)
Functional Keywordsinhibitor, oxidoreductase, oxidoreductase-inhibitor complex, oxidoreductase/inhibitor
Biological sourceHomo sapiens (human)
Total number of polymer chains4
Total formula weight185342.60
Authors
Geeraerts, Z.,Yeh, S.-R. (deposition date: 2024-02-15, release date: 2024-08-21, Last modification date: 2024-09-11)
Primary citationGeeraerts, Z.,Ishigami, I.,Lewis-Ballester, A.,Pham, K.N.,Kozlova, A.,Mathieu, C.,Frederick, R.,Yeh, S.R.
Structural Insights into Protein-Inhibitor Interactions in Human Tryptophan Dioxygenase.
J.Med.Chem., 67:14543-14552, 2024
Cited by
PubMed Abstract: Human tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are two important targets in cancer immunotherapy. Extensive research has led to a large number of potent IDO inhibitors; in addition, 52 structures of IDO in complex with inhibitors with a wide array of chemical scaffolds have been documented. In contrast, progress in the development of TDO inhibitors has been limited. Only four structures of TDO in complex with competitive inhibitors that compete with the substrate L-tryptophan for binding to the active site have been reported to date. Here we systematically evaluated the structures of TDO in complex with competitive inhibitors with three types of pharmacophores, imidazo-isoindole, indole-tetrazole, and indole-benzotriazole. The comparative assessment of the protein-inhibitor interactions sheds new light into the structure-based design of enzyme-selective inhibitors.
PubMed: 39106326
DOI: 10.1021/acs.jmedchem.4c01360
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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PDB entries from 2024-11-20

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