4qx4
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Human Aldose Reductase complexed with a ligand with a new scaffold at 1.26 A== |
| + | <StructureSection load='4qx4' size='340' side='right' caption='[[4qx4]], [[Resolution|resolution]] 1.26Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qx4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QX4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3E2:(3-THIOXO-2,3-DIHYDRO-5H-[1,2,4]TRIAZINO[5,6-B]INDOL-5-YL)ACETIC+ACID'>3E2</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us0|1us0]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=4qx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qx4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qx4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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 == | ||
| + | Fifteen compounds, sharing an indole-1-acetic acid moiety as a common fragment, were selected from commercial databases for testing aldose reductase inhibition. 3-Mercapto-5H-1,2,4-triazino[5,6-b]indole-5-acetic acid (13) was the most promising inhibitor, with an IC50 in the submicromolar range and high selectivity, relative to aldehyde reductase. The crystal structure of aldose reductase complexed with 13 revealed an interaction pattern explaining its high affinity. Physicochemical parameters underline the excellent "leadlikeness" of 13 as a promising candidate for further structure optimizations. | ||
| - | + | Identification of novel aldose reductase inhibitors based on carboxymethylated mercaptotriazinoindole scaffold.,Stefek M, Soltesova Prnova M, Majekova M, Rechlin C, Heine A, Klebe G J Med Chem. 2015 Mar 26;58(6):2649-57. doi: 10.1021/jm5015814. Epub 2015 Mar 4. PMID:25695864<ref>PMID:25695864</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aldehyde reductase]] | ||
[[Category: Heine, A]] | [[Category: Heine, A]] | ||
| + | [[Category: Klebe, G]] | ||
[[Category: Rechlin, C]] | [[Category: Rechlin, C]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| + | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | ||
| + | [[Category: Tim barrel]] | ||
Revision as of 13:10, 1 April 2015
Human Aldose Reductase complexed with a ligand with a new scaffold at 1.26 A
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