7wt2: Difference between revisions
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<StructureSection load='7wt2' size='340' side='right'caption='[[7wt2]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='7wt2' size='340' side='right'caption='[[7wt2]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7wt2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wt2]] is a 2 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=7WT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ZO:(~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic+acid'>5ZO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ZO:(~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic+acid'>5ZO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7wt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt2 OCA], [https://pdbe.org/7wt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt2 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt2 ProSAT]</span></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=7wt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt2 OCA], [https://pdbe.org/7wt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt2 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LGUL_HUMAN LGUL_HUMAN] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B.<ref>PMID:19199007</ref> | |||
<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 7wt2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7wt2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Usami | [[Category: Usami M]] | ||
[[Category: Yokoyama | [[Category: Yokoyama H]] | ||
Latest revision as of 20:44, 29 November 2023
human glyoxalase I in complex with TLSC702human glyoxalase I in complex with TLSC702
Structural highlights
FunctionLGUL_HUMAN Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B.[1] Publication Abstract from PubMedHuman glyoxalase I (hGLO I) is an enzyme for detoxification of methylglyoxal (MG) and has been considered an attractive target for the development of new anticancer drugs. In our previous report, the GLO I inhibitor TLSC702 induced apoptosis in tumor cells. Here, we determined the crystal structures of hGLO I and its complex with TLSC702. In the complex, the carboxyl O atom of TLSC702 is coordinated to Zn(2+) , and TLSC702 mainly shows van der Waals interaction with hydrophobic residues. In the inhibitor-unbound structure, glycerol, which has similar functional groups to MG, was bound to Zn(2+) , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs. Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.,Usami M, Ando K, Shibuya A, Takasawa R, Yokoyama H FEBS Lett. 2022 Apr 1. doi: 10.1002/1873-3468.14344. PMID:35363883[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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