4jir
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jir]] 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=4JIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JIR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jir]] 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=4JIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JIR FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPR:{5-[(2E)-2-METHYL-3-PHENYLPROP-2-EN-1-YLIDENE]-4-OXO-2-THIOXO-1,3-THIAZOLIDIN-3-YL}ACETIC+ACID'>EPR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPR:{5-[(2E)-2-METHYL-3-PHENYLPROP-2-EN-1-YLIDENE]-4-OXO-2-THIOXO-1,3-THIAZOLIDIN-3-YL}ACETIC+ACID'>EPR</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=4jir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jir OCA], [https://pdbe.org/4jir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jir RCSB], [https://www.ebi.ac.uk/pdbsum/4jir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jir ProSAT]</span></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=4jir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jir OCA], [https://pdbe.org/4jir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jir RCSB], [https://www.ebi.ac.uk/pdbsum/4jir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jir ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | [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. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The antineoplastic target aldo-keto reductase family member 1B10 (AKR1B10) and the critical polyol pathway enzyme aldose reductase (AKR1B1) share high structural similarity. Crystal structures reported here reveal a surprising Trp112 native conformation stabilized by a specific Gln114-centered hydrogen bond network in the AKR1B10 holoenzyme, and suggest that AKR1B1 inhibitors could retain their binding affinities toward AKR1B10 by inducing Trp112 flip to result in an "AKR1B1-like" active site in AKR1B10, while selective AKR1B10 inhibitors can take advantage of the broader active site of AKR1B10 provided by the native Trp112 side-chain orientation. | ||
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| - | Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111).,Zhang L, Zhang H, Zhao Y, Li Z, Chen S, Zhai J, Chen Y, Xie W, Wang Z, Li Q, Zheng X, Hu X FEBS Lett. 2013 Oct 4. pii: S0014-5793(13)00726-6. doi:, 10.1016/j.febslet.2013.09.031. PMID:24100137<ref>PMID:24100137</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4jir" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | *[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And Epalrestat
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Categories: Homo sapiens | Large Structures | Chen K | Hu X | Zhai J | Zhang H | Zhang L | Zhao Y | Zheng X
