4qxi
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of human AR complexed with NADP+ and AK198== |
| + | <StructureSection load='4qxi' size='340' side='right' caption='[[4qxi]], [[Resolution|resolution]] 0.87Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qxi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QXI FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I98:{2-[(4-AMINO-2-FLUOROBENZYL)CARBAMOYL]-5-CHLOROPHENOXY}ACETIC+ACID'>I98</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]], [[2iki|2iki]]</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=4qxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qxi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qxi RCSB], [http://www.ebi.ac.uk/pdbsum/4qxi 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 == | ||
| + | The effect of halogen-to-hydrogen bond substitution on the binding energetics and biological activity of a human aldose reductase inhibitor has been studied using X-ray crystallography, IC50 measurements, advanced binding free energy calculations, and simulations. The replacement of Br or I atoms by an amine (NH2) group has not induced changes in the original geometry of the complex, which made it possible to study the isolated features of selected noncovalent interactions in a biomolecular complex. | ||
| - | The | + | The Effect of Halogen-to-Hydrogen Bond Substitution on Human Aldose Reductase Inhibition.,Fanfrlik J, Ruiz FX, Kadlcikova A, Rezac J, Cousido-Siah A, Mitschler A, Haldar S, Lepsik M, Kolar MH, Majer P, Podjarny AD, Hobza P ACS Chem Biol. 2015 Jul 17;10(7):1637-42. doi: 10.1021/acschembio.5b00151. Epub, 2015 May 6. PMID:25919404<ref>PMID:25919404</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Aldehyde reductase]] | ||
[[Category: Cousido-Siah, A]] | [[Category: Cousido-Siah, A]] | ||
| + | [[Category: Fanfrlik, J]] | ||
[[Category: Hobza, P]] | [[Category: Hobza, P]] | ||
| - | [[Category: Ruiz, F | + | [[Category: Mitschler, A]] |
| - | [[Category: | + | [[Category: Podjarny, A D]] |
| + | [[Category: Ruiz, F X]] | ||
| + | [[Category: Aldose reductase]] | ||
| + | [[Category: Cytosolic]] | ||
| + | [[Category: Diabetes]] | ||
| + | [[Category: Halogenated compound]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Tim barrel]] | ||
Revision as of 14:05, 22 July 2015
Crystal structure of human AR complexed with NADP+ and AK198
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