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4q3f

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==Human D-DT complexed with tartrate==
==Human D-DT complexed with tartrate==
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<StructureSection load='4q3f' size='340' side='right' caption='[[4q3f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4q3f' size='340' side='right'caption='[[4q3f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q3f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q3F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q3f]] 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=4Q3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q3F FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-dopachrome_decarboxylase D-dopachrome decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.84 4.1.1.84] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q3f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q3f RCSB], [http://www.ebi.ac.uk/pdbsum/4q3f PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q3f OCA], [https://pdbe.org/4q3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q3f RCSB], [https://www.ebi.ac.uk/pdbsum/4q3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q3f ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DOPD_HUMAN DOPD_HUMAN] Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
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We report a new inflammatory activity for extracellular d-dopachrome tautomerase (D-DT), the recruitment of neutrophils to the lung on D-DT intratracheal installation of C57BL/6J mice with an EC50 of 5.6 mug. We also find that D-DT and macrophage migration inhibitory factor (MIF) have additive effects in neutrophil recruitment. Although the tautomerase site of D-DT and its homologue MIF are biophysically very different, 4-iodo-6-phenylpyrimidine (4-IPP) forms a covalent bond with Pro-1 of both proteins, resulting in a 6-phenylpyrimidine (6-PP) adduct. Recruitment of neutrophils to the lung for the 6-PP adducts of D-DT and MIF are reduced by approximately 50% relative to the apo proteins, demonstrating that an unmodified Pro-1 is important for this activity, but there is no cooperativity in inhibition of the proteins together. The differences in the binding mode of the 6-PP adduct for D-DT was determined by crystallographic studies at 1.13 A resolution and compared to the structure of the MIF-6-PP complex. There are major differences in the location of the 6-PP adduct to the D-DT and MIF active sites that provide insight into the lack of cooperativity by 4-IPP and into tuning the properties of the covalent inhibitors of D-DT and MIF that are necessary for the development of therapeutic small molecules against neutrophil damage from lung infections such as Pseudomonas aeruginosa in cystic fibrosis and immunocompromised patients.-Rajasekaran, D., Zierow, S., Syed, M., Bucala, R., Bhandari, V., Lolis, E. J. Targeting distinct tautomerase sites of D-DT and MIF with a single molecule for inhibition of neutrophil lung recruitment.
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Targeting distinct tautomerase sites of D-DT and MIF with a single molecule for inhibition of neutrophil lung recruitment.,Rajasekaran D, Zierow S, Syed M, Bucala R, Bhandari V, Lolis EJ FASEB J. 2014 Jul 11. pii: fj.14-256636. PMID:25016026<ref>PMID:25016026</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Macrophage inhibitory factor 3D structures|Macrophage inhibitory factor 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: D-dopachrome decarboxylase]]
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[[Category: Homo sapiens]]
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[[Category: Lolis, E.]]
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[[Category: Large Structures]]
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[[Category: Rajasekaran, D.]]
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[[Category: Lolis E]]
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[[Category: Cd74]]
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[[Category: Rajasekaran D]]
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[[Category: Lyase]]
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[[Category: Tautomerase]]
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Current revision

Human D-DT complexed with tartrate

PDB ID 4q3f

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