1dpt: Difference between revisions

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 <StructureSection load='1dpt' size='340' side='right'caption='[[1dpt]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dpt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dpt]] 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=1DPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPT FirstGlance]. <br>
-</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=1dpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpt OCA], [https://pdbe.org/1dpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpt RCSB], [https://www.ebi.ac.uk/pdbsum/1dpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpt ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54&#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=1dpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpt OCA], [https://pdbe.org/1dpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpt RCSB], [https://www.ebi.ac.uk/pdbsum/1dpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpt 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).
+[https://www.uniprot.org/uniprot/DOPD_HUMAN DOPD_HUMAN] Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpt ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-D-Dopachrome tautomerase shares a low homologous amino acid sequence (33% homology) with the macrophage migration inhibitory factor (MIF) and possesses similar tautomerase activity as well. MIF is a cytokine involved in inflammatory reactions and immune responses. Whereas recent studies have identified MIF as a pituitary hormone and immunoregulator, much less is known about the structural basis of these physiological functions and the real significance of tautomerase activity. Therefore, interest in the structure-function relationship between D-dopachrome tautomerase and MIF has increased, especially with regard to inflammation and immune responses. We have determined the X-ray crystal structure of human D-dopachrome tautomerase at 1.54 A resolution. D-Dopachrome tautomerase folds to form a homotrimer that has extensive contact between subunits by intersubunit beta-sheets. Its overall topology and trimeric formations are similar to those of human MIF. The N-terminal proline is located at the bottom of a positively charged pocket in which the conformations of Lys32 and Ser63 are highly conserved. These positively charged properties are also seen in the active site pocket of human MIF, bacterial 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI), and 4-oxalocrotonate tautomerase (4-OT). A detailed comparison of these structures revealed significant differences in the environment around the potential active site, the intersubunit contacts, and charge distribution on the molecular surface. It can be concluded that these features are related to the physiological role and tautomerase activity of MIF and D-dopachrome tautomerase. The present structural study could be helpful for designing effective inhibitors that modulate immunoregulatory and hormone-like effects.
-Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution.,Sugimoto H, Taniguchi M, Nakagawa A, Tanaka I, Suzuki M, Nishihira J Biochemistry. 1999 Mar 16;38(11):3268-79. PMID:10079069<ref>PMID:10079069</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dpt" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Macrophage inhibitory factor 3D structures|Macrophage inhibitory factor 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Nakagawa, A]]
+[[Category: Nakagawa A]]
-[[Category: Sugimoto, H]]
+[[Category: Sugimoto H]]
-[[Category: Tanaka, I]]
+[[Category: Tanaka I]]
-[[Category: Taniguchi, M]]
+[[Category: Taniguchi M]]
-[[Category: Cytokine]]
-[[Category: Growth factor]]
-[[Category: Tautomerase]]