4x2a: Difference between revisions
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''' | ==Crystal structure of mouse glyoxalase I complexed with baicalein== | ||
<StructureSection load='4x2a' size='340' side='right' caption='[[4x2a]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4x2a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X2A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3WL:5,6,7-TRIHYDROXY-2-PHENYL-4H-CHROMEN-4-ONE'>3WL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za0|2za0]], [[4kyk|4kyk]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2a OCA], [http://pdbe.org/4x2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x2a RCSB], [http://www.ebi.ac.uk/pdbsum/4x2a PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LGUL_MOUSE LGUL_MOUSE]] 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 (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The antitumor pharmacological property of flavonoids is correlated with inhibition towards glyoxalase I (GLOI), a critical zinc-enzyme in the methylglyoxal detoxification pathway. In this study, 16 flavonoids were examined, and only baicalein (Ki of 0.183 microM) is identified as a potent in vitro GLOI inhibitor. X-ray crystallographic analysis reveals that baicalein chelates with the catalytic Zn(2+) via its characteristic C6/C7 hydroxyl groups. The coordination ability of flavonoids, and therefore their ability to inhibit GLOI, is determined by the Zn(2+) coordination geometry, the rigid skeleton of flavonoids and the geometry of the hydrophobic cavity of the GLOI active site. This structural basis could be useful in predicting GLOI inhibition of other natural polyphenols. | |||
In Vitro Inhibition of Glyoxalase capital I, Ukrainian by Flavonoids: New Insights from Crystallographic Analysis.,Zhang H, Zhai J, Zhang L, Li C, Zhao Y, Chen Y, Li Q, Hu XP Curr Top Med Chem. 2016;16(4):460-6. PMID:26268338<ref>PMID:26268338</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4x2a" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactoylglutathione lyase]] | |||
[[Category: Hu, X]] | |||
[[Category: Li, C]] | |||
[[Category: Zhai, J]] | |||
[[Category: Zhang, H]] | [[Category: Zhang, H]] | ||
[[Category: Zhang, L]] | [[Category: Zhang, L]] | ||
[[Category: Zhao, Y]] | [[Category: Zhao, Y]] | ||
[[Category: | [[Category: Lyase]] | ||
[[Category: | [[Category: Lyase-lyase inhibitor complex]] | ||
Revision as of 23:38, 30 November 2015
Crystal structure of mouse glyoxalase I complexed with baicaleinCrystal structure of mouse glyoxalase I complexed with baicalein
Structural highlights
Function[LGUL_MOUSE] 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 (By similarity). Publication Abstract from PubMedThe antitumor pharmacological property of flavonoids is correlated with inhibition towards glyoxalase I (GLOI), a critical zinc-enzyme in the methylglyoxal detoxification pathway. In this study, 16 flavonoids were examined, and only baicalein (Ki of 0.183 microM) is identified as a potent in vitro GLOI inhibitor. X-ray crystallographic analysis reveals that baicalein chelates with the catalytic Zn(2+) via its characteristic C6/C7 hydroxyl groups. The coordination ability of flavonoids, and therefore their ability to inhibit GLOI, is determined by the Zn(2+) coordination geometry, the rigid skeleton of flavonoids and the geometry of the hydrophobic cavity of the GLOI active site. This structural basis could be useful in predicting GLOI inhibition of other natural polyphenols. In Vitro Inhibition of Glyoxalase capital I, Ukrainian by Flavonoids: New Insights from Crystallographic Analysis.,Zhang H, Zhai J, Zhang L, Li C, Zhao Y, Chen Y, Li Q, Hu XP Curr Top Med Chem. 2016;16(4):460-6. PMID:26268338[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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