1iei

<StructureSection load='1iei' size='340' side='right' caption='[[1iei]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1iei]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZES:[3-(4-BROMO-2-FLUORO-BENZYL)-7-CHLORO-2,4-DIOXO-3,4-DIHYDRO-2H-QUINAZOLIN-1-YL]-ACETIC+ACID'>ZES</scene></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=1iei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iei OCA], [http://pdbe.org/1iei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iei RCSB], [http://www.ebi.ac.uk/pdbsum/1iei PDBsum]</span></td></tr>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/1iei_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The crystal structure of the complex of human recombinant aldose reductase (AR) with zenarestat, one of its potent inhibitors, has been solved at 2.5 A resolution. Zenarestat fits neatly in the hydrophobic active site and induces unique and dramatic conformational changes. For example, the benzene ring of zenarestat occupies a gap in the side chains of Leu300 and Trp111 that interact directly and forms a CH-pi interaction in the native holoenzyme. As a result, the benzene ring of the inhibitor and these side chains form a CH-pi-pi interaction. Such structural information is key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics.

The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.,Kinoshita T, Miyake H, Fujii T, Takakura S, Goto T Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):622-6. Epub 2002, Mar 22. PMID:11914486<ref>PMID:11914486</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1iei" style="background-color:#fffaf0;"></div>

*[[Aldose Reductase|Aldose Reductase]]

[[Category: Aldehyde reductase]]

[[Category: Human]]

[[Category: Fujii, T]]

[[Category: Goto, T]]

[[Category: Kinoshita, T]]

[[Category: Miyake, H]]

[[Category: Takakura, S]]

[[Category: Protein-inhibitor complex]]