2iq0: Difference between revisions

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-{{Seed}}
-[[Image:2iq0.png|left|200px]]
-<!--
+==Crystal Structure of Aldose Reductase complexed with Hexanoic Acid==
-The line below this paragraph, containing "STRUCTURE_2iq0", creates the "Structure Box" on the page.
+<StructureSection load='2iq0' size='340' side='right'caption='[[2iq0]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2iq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IQ0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6NA:HEXANOIC+ACID'>6NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-{{STRUCTURE_2iq0|  PDB=2iq0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iq0 OCA], [https://pdbe.org/2iq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iq0 RCSB], [https://www.ebi.ac.uk/pdbsum/2iq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iq0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
+== 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/iq/2iq0_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=2iq0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The competitive inhibition constants of series of inhibitors related to phenylacetic acid against both wild-type and the doubly mutanted C298A/W219Y aldose reductase have been measured. Van't Hoff analysis shows that these acids bind with an enthalpy near -6.8 kcal/mol derived from the electrostatic interactions, while the 100-fold differences in binding affinity appear to be largely due to entropic factors that result from differences in conformational freedom in the unbound state. These temperature studies also point out the difference between substrate and inhibitor binding. X-ray crystallographic analysis of a few of these inhibitor complexes both confirms the importance of a previously described anion binding site and reveals the hydrophobic nature of the primary binding site and its general plasticity. Based on these results, N-glycylthiosuccinimides were synthesized to demonstrate their potential in studies that probe distal binding sites. Reduced alpha-lipoic acid, an anti-oxidant and therapeutic for diabetic complications, was shown to bind aldose reductase with a binding constant of 1 microM.
-===Crystal Structure of Aldose Reductase complexed with Hexanoic Acid===
+Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes.,Brownlee JM, Carlson E, Milne AC, Pape E, Harrison DH Bioorg Chem. 2006 Dec;34(6):424-44. Epub 2006 Nov 2. PMID:17083960<ref>PMID:17083960</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iq0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17083960}}, adds the Publication Abstract to the page
+*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17083960 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17083960}}
+__TOC__
+</StructureSection>
-==About this Structure==
-IQ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IQ0 OCA].
-==Reference==
-Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes., Brownlee JM, Carlson E, Milne AC, Pape E, Harrison DH, Bioorg Chem. 2006 Dec;34(6):424-44. Epub 2006 Nov 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17083960 17083960]
-[[Category: Aldehyde reductase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Brownlee, J M.]]
+[[Category: Brownlee JM]]
-[[Category: Harrison, D H.T.]]
+[[Category: Harrison DHT]]
-[[Category: Aldo-keto reductase]]
-[[Category: Ari]]
-[[Category: Tim-barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:51:38 2008''