9b1q
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PYN1 inhibitor== | |
| + | <StructureSection load='9b1q' size='340' side='right'caption='[[9b1q]], [[Resolution|resolution]] 2.62Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9b1q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9B1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9B1Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.624Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9b1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9b1q OCA], [https://pdbe.org/9b1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9b1q RCSB], [https://www.ebi.ac.uk/pdbsum/9b1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9b1q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/T23O_HUMAN T23O_HUMAN] Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Structural Insights into Protein-Inhibitor Interactions in Human Tryptophan Dioxygenase.,Geeraerts Z, Ishigami I, Lewis-Ballester A, Pham KN, Kozlova A, Mathieu C, Frederick R, Yeh SR J Med Chem. 2024 Aug 6. doi: 10.1021/acs.jmedchem.4c01360. PMID:39106326<ref>PMID:39106326</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Geeraerts | + | <div class="pdbe-citations 9b1q" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yeh | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Geeraerts Z]] | ||
| + | [[Category: Yeh S-R]] | ||
Current revision
Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PYN1 inhibitor
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