Summary for 7LU7
| Entry DOI | 10.2210/pdb7lu7/pdb |
| Descriptor | Tryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE, alpha-methyl-L-tryptophan, ... (5 entities in total) |
| Functional Keywords | human tdo, human tdo2, htdo, htdo2, nlg919, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 185198.62 |
| Authors | Yeh, S.-R. (deposition date: 2021-02-21, release date: 2022-08-24, Last modification date: 2024-08-28) |
| Primary citation | Geeraerts, 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., 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: 39106326DOI: 10.1021/acs.jmedchem.4c01360 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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