Structural highlights
7a62 is a 4 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 6tue. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Gene: | IDO1, IDO, INDO (HUMAN) |
| Activity: | Indoleamine 2,3-dioxygenase, with EC number 1.13.11.52 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[I23O1_HUMAN] Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.[1]
Publication Abstract from PubMed
Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutic target in cancer research. Its structure includes a loop, named the JK-loop, that controls the orientation of the substrate or inhibitor within the active site. However, little has been reported about the crystal structure of this loop. In the present work, the conformation of the JK-loop is determined for the first time in the presence of the heme cofactor in the active site through X-ray diffraction experiments (2.44 A resolution). Molecular-dynamics trajectories were also obtained to provide dynamic information about the loop according to the presence of cofactor. This new structural and dynamic information highlights the importance of the JK-loop in confining the labile heme cofactor to the active site.
Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine 2,3-dioxygenase 1.,Mirgaux M, Leherte L, Wouters J Acta Crystallogr D Struct Biol. 2020 Dec 1;76(Pt 12):1211-1221. doi:, 10.1107/S2059798320013510. Epub 2020 Nov 19. PMID:33263327[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 2007 Aug 1;67(15):7082-7. PMID:17671174 doi:http://dx.doi.org/10.1158/0008-5472.CAN-07-1872
- ↑ Mirgaux M, Leherte L, Wouters J. Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine 2,3-dioxygenase 1. Acta Crystallogr D Struct Biol. 2020 Dec 1;76(Pt 12):1211-1221. doi:, 10.1107/S2059798320013510. Epub 2020 Nov 19. PMID:33263327 doi:http://dx.doi.org/10.1107/S2059798320013510
