3v35: Difference between revisions

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==Aldose reductase complexed with a nitro compound==
==Aldose reductase complexed with a nitro compound==
<StructureSection load='3v35' size='340' side='right' caption='[[3v35]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3v35' size='340' side='right' caption='[[3v35]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKR1B1, ALDR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=3v35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v35 RCSB], [http://www.ebi.ac.uk/pdbsum/3v35 PDBsum]</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=3v35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v35 OCA], [http://pdbe.org/3v35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v35 RCSB], [http://www.ebi.ac.uk/pdbsum/3v35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v35 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3v35" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Revision as of 02:17, 6 August 2016

Aldose reductase complexed with a nitro compoundAldose reductase complexed with a nitro compound

Structural highlights

3v35 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:AKR1B1, ALDR1 (HUMAN)
Activity:Aldehyde reductase, with EC number 1.1.1.21
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Publication Abstract from PubMed

A little is more than enough: Aldose reductase (AR) is a potential target in a wide range of diseases but its utility may be limited by the side effects caused by complete inhibition. Furthermore, known inhibitors of AR have suffered in clinical evaluation due to poor bioavailability. Here, the clinically used antiprotozoal drug nitazoxanide with proven bioavailability has been shown to partially inhibit AR, potentially circumventing the negatives effects of complete enzyme inhibition.

Partial Inhibition of Aldose Reductase by Nitazoxanide and Its Molecular Basis.,Zheng X, Zhang L, Chen W, Chen Y, Xie W, Hu X ChemMedChem. 2012 Aug 13. doi: 10.1002/cmdc.201200333. PMID:22890894[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Zheng X, Zhang L, Chen W, Chen Y, Xie W, Hu X. Partial Inhibition of Aldose Reductase by Nitazoxanide and Its Molecular Basis. ChemMedChem. 2012 Aug 13. doi: 10.1002/cmdc.201200333. PMID:22890894 doi:10.1002/cmdc.201200333

3v35, resolution 1.90Å

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