8dbb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of DDT with the selective inhibitor 2,5-Pyridinedicarboxylic Acid== | |
| + | <StructureSection load='8dbb' size='340' side='right'caption='[[8dbb]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8dbb]] is a 3 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=8DBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DBB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=R3K:pyridine-2,5-dicarboxylic+acid'>R3K</scene></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=8dbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dbb OCA], [https://pdbe.org/8dbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dbb RCSB], [https://www.ebi.ac.uk/pdbsum/8dbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dbb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DOPD_HUMAN DOPD_HUMAN] Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Macrophage migration inhibitory factor (MIF) and D-dopachrome tautomerase (D-DT) are two pleotropic cytokines, which are coexpressed in various cell types to activate the cell surface receptor CD74. Via the MIF/CD74 and D-DT/CD74 axes, the two proteins exhibit either beneficial or deleterious effect on human diseases. In this study, we report the identification of 2,5-pyridinedicarboxylic acid (a.k.a. 1) that effectively blocks the D-DT-induced activation of CD74 and demonstrates an impressive 79-fold selectivity for D-DT over MIF. Crystallographic characterization of D-DT-1 elucidates the binding features of 1 and reveals previously unrecognized differences between the MIF and D-DT active sites that explain the ligand's functional selectivity. The commercial availability, low cost, and high selectivity make 1 the ideal tool for studying the pathophysiological functionality of D-DT in disease models. At the same time, our comprehensive biochemical, computational, and crystallographic analyses serve as a guide for generating highly potent and selective D-DT inhibitors. | ||
| - | + | 2,5-Pyridinedicarboxylic acid is a bioactive and highly selective inhibitor of D-dopachrome tautomerase.,Parkins A, Das P, Prahaladan V, Rangel VM, Xue L, Sankaran B, Bhandari V, Pantouris G Structure. 2023 Mar 2;31(3):355-367.e4. doi: 10.1016/j.str.2023.01.008. Epub 2023 , Feb 17. PMID:36805127<ref>PMID:36805127</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8dbb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Banumathi S]] | ||
| + | [[Category: Pantouris G]] | ||
| + | [[Category: Parkins A]] | ||
Revision as of 07:34, 8 March 2023
Crystal structure of DDT with the selective inhibitor 2,5-Pyridinedicarboxylic Acid
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