View source for 7wsz


==human glyoxalase I (with C-ter His tag) in glycerol-bound form==
<StructureSection load='7wsz' size='340' side='right'caption='[[7wsz]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wsz]] 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=7WSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WSZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=7wsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wsz OCA], [https://pdbe.org/7wsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wsz RCSB], [https://www.ebi.ac.uk/pdbsum/7wsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wsz ProSAT]</span></td></tr>
</table>
== 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;">
== Publication Abstract from PubMed ==
Human 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<ref>PMID:35363883</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wsz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ando K]]
[[Category: Usami M]]
[[Category: Yokoyama H]]