4q3f: Difference between revisions
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<StructureSection load='4q3f' size='340' side='right'caption='[[4q3f]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4q3f' size='340' side='right'caption='[[4q3f]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q3f]] is a 3 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene | </td></tr><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> | ||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4q3f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4q3f" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Macrophage inhibitory factor 3D structures|Macrophage inhibitory factor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lolis | [[Category: Lolis E]] | ||
[[Category: Rajasekaran | [[Category: Rajasekaran D]] | ||
Revision as of 10:42, 8 February 2023
Human D-DT complexed with tartrateHuman D-DT complexed with tartrate
Structural highlights
FunctionDOPD_HUMAN Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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