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'''Unreleased structure'''


The entry 8vug is ON HOLD  until Paper Publication
==Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PPN1 inhibitor==
<StructureSection load='8vug' size='340' side='right'caption='[[8vug]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vug]] 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=8VUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VUG 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]] 2.05&#8491;</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=8vug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vug OCA], [https://pdbe.org/8vug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vug RCSB], [https://www.ebi.ac.uk/pdbsum/8vug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vug 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.


Authors: Geeraerts, Z., Yeh, S.
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>


Description: Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PPN1 inhibitor
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Geeraerts, Z]]
<div class="pdbe-citations 8vug" style="background-color:#fffaf0;"></div>
[[Category: Yeh, S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Geeraerts Z]]
[[Category: Yeh S]]
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