3s3g
From Proteopedia
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| - | [[Image:3s3g.png|left|200px]] | ||
| - | + | ==Crystal Structure of Human Aldose Reductase Complexed with Tolmetin== | |
| + | <StructureSection load='3s3g' size='340' side='right'caption='[[3s3g]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3s3g]] 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=3S3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S3G 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]] 1.8Å</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=TLT:TOLMETIN'>TLT</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=3s3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s3g OCA], [https://pdbe.org/3s3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s3g RCSB], [https://www.ebi.ac.uk/pdbsum/3s3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s3g 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 3s3g" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Aldose | + | *[[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]] | |
| - | + | ||
Current revision
Crystal Structure of Human Aldose Reductase Complexed with Tolmetin
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Categories: Homo sapiens | Large Structures | Chen J | Hu X | Luo H | Zheng X
