3cv7: Difference between revisions

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New page: '''Unreleased structure''' The entry 3cv7 is ON HOLD until Paper Publication Authors: Carbone, V., El-Kabbani, O. Description: Crystal structure of porcine aldehyde reductase ternary c...
 
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'''Unreleased structure'''


The entry 3cv7 is ON HOLD  until Paper Publication
==Crystal structure of porcine aldehyde reductase ternary complex==
<StructureSection load='3cv7' size='340' side='right'caption='[[3cv7]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3cv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CV7 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]] 2.412&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2U:3,5-DICHLORO-2-HYDROXYBENZOIC+ACID'>C2U</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3cv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cv7 OCA], [https://pdbe.org/3cv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cv7 RCSB], [https://www.ebi.ac.uk/pdbsum/3cv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cv7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AK1A1_PIG AK1A1_PIG] 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. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cv7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3cv7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of aldehyde reductase (ALR1) in ternary complex with the coenzyme NADPH and 3,5-dichlorosalicylic acid (DCL), a potent inhibitor of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1), was determined at a resolution of 2.41A. The inhibitor formed a network of hydrogen bonds with the active site residues Trp22, Tyr50, His113, Trp114 and Arg312. Molecular modelling calculations together with inhibitory activity measurements indicated that DCL was a less potent inhibitor of ALR1 (256-fold) when compared to AKR1C1. In AKR1C1, the inhibitor formed a 10-fold stronger binding interaction with the catalytic residue (Tyr55), non-conserved hydrogen bonding interaction with His222, and additional van der Waals contacts with the non-conserved C-terminal residues Leu306, Leu308 and Phe311 that contribute to the inhibitor's selectivity advantage for AKR1C1 over ALR1.


Authors: Carbone, V., El-Kabbani, O.
Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor 3,5-dichlorosalicylic acid: implications for inhibitor binding and selectivity.,Carbone V, Chung R, Endo S, Hara A, El-Kabbani O Arch Biochem Biophys. 2008 Nov 1;479(1):82-7. Epub 2008 Aug 28. PMID:18782556<ref>PMID:18782556</ref>


Description: Crystal structure of porcine aldehyde reductase ternary complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3cv7" style="background-color:#fffaf0;"></div>


 
==See Also==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:34:28 2008''
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Carbone V]]
[[Category: El-Kabbani O]]
Retrieved from "https://proteopedia.org/3cv7"