2alr

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[[Image:2alr.gif|left|200px]]
 
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==ALDEHYDE REDUCTASE==
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The line below this paragraph, containing "STRUCTURE_2alr", creates the "Structure Box" on the page.
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<StructureSection load='2alr' size='340' side='right'caption='[[2alr]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2alr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1alr 1alr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2alr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2alr OCA], [https://pdbe.org/2alr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2alr RCSB], [https://www.ebi.ac.uk/pdbsum/2alr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2alr ProSAT]</span></td></tr>
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{{STRUCTURE_2alr| PDB=2alr | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AK1A1_HUMAN AK1A1_HUMAN] Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN).<ref>PMID:10510318</ref> <ref>PMID:11306097</ref> <ref>PMID:18276838</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/2alr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2alr ConSurf].
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<div style="clear:both"></div>
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'''ALDEHYDE REDUCTASE'''
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==See Also==
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*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
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__TOC__
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</StructureSection>
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==About this Structure==
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2ALR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1alr 1alr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALR OCA].
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==Reference==
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Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications., El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ, Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299353 15299353]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: El-Kabbani, O.]]
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[[Category: El-Kabbani O]]
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[[Category: Oxidoreductase]]
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[[Category: Tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:11:51 2008''
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Current revision

ALDEHYDE REDUCTASE

PDB ID 2alr

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