3rx3: Difference between revisions
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== | ==Crystal Structure of Human Aldose Reductase Complexed with Sulindac== | ||
[[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN | <StructureSection load='3rx3' size='340' side='right'caption='[[3rx3]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rx3]] is a 1 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=3RX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RX3 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SUZ:[(1Z)-5-FLUORO-2-METHYL-1-{4-[METHYLSULFINYL]BENZYLIDENE}-1H-INDEN-3-YL]ACETIC+ACID'>SUZ</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=3rx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rx3 OCA], [https://pdbe.org/3rx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rx3 RCSB], [https://www.ebi.ac.uk/pdbsum/3rx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rx3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sulindac (SLD) exhibits both the highest inhibitory activity towards human aldose reductase (AR) among popular non-steroidal anti-inflammatory drugs and clear beneficial clinical effects on Type 2 diabetes. However, the molecular basis for these properties is unclear. Here, we report that SLD and its pharmacologically active/inactive metabolites, SLD sulfide and SLD sulfone, are equally effective as un-competitive inhibitors of AR in vitro. Crystallographic analysis reveals that pi-pi stacking favored by the distinct scaffold of SLDs is pivotal to their high AR inhibitory activities. These results also suggest that SLD sulfone could be a potent lead compound for AR inhibition in vivo. | |||
The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase.,Zheng X, Zhang L, Zhai J, Chen Y, Luo H, Hu X FEBS Lett. 2012 Jan 2;586(1):55-9. Epub 2011 Dec 8. PMID:22155003<ref>PMID:22155003</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[ | <div class="pdbe-citations 3rx3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chen | [[Category: Large Structures]] | ||
[[Category: Hu | [[Category: Chen J]] | ||
[[Category: Luo | [[Category: Hu X]] | ||
[[Category: Zheng | [[Category: Luo H]] | ||
[[Category: Zheng X]] | |||
Latest revision as of 17:20, 1 November 2023
Crystal Structure of Human Aldose Reductase Complexed with Sulindac
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