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New page: left|200px<br /> <applet load="1sg0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sg0, resolution 1.50Å" /> '''Crystal structure a...
 
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[[Image:1sg0.gif|left|200px]]<br />
<applet load="1sg0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sg0, resolution 1.50&Aring;" />
'''Crystal structure analysis of QR2 in complex with resveratrol'''<br />


==Overview==
==Crystal structure analysis of QR2 in complex with resveratrol==
Resveratrol has been shown to have chemopreventive, cardioprotective, and, antiaging properties. Here, we report that resveratrol is a potent, inhibitor of quinone reductase 2 (QR2) activity in vitro with a, dissociation constant of 35 nM and show that it specifically binds to the, deep active-site cleft of QR2 using high-resolution structural analysis., All three resveratrol hydroxyl groups form hydrogen bonds with amino acids, from QR2, anchoring a flat resveratrol molecule in parallel with the, isoalloxazine ring of FAD. The unique active-site pocket in QR2 could, potentially bind other natural polyphenols such as flavonoids, as proven, by the high affinity exhibited by quercetin toward QR2. K562 cells with, QR2 expression suppressed by RNAi showed similar properties as, resveratrol-treated cells in their resistance to quinone toxicity., Furthermore, the QR2 knockdown K562 cells exhibit increased antioxidant, and detoxification enzyme expression and reduced proliferation rates., These observations could imply that the chemopreventive and, cardioprotective properties of resveratrol are possibly the results of QR2, activity inhibition, which in turn, up-regulates the expression of, cellular antioxidant enzymes and cellular resistance to oxidative stress.
<StructureSection load='1sg0' size='340' side='right'caption='[[1sg0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sg0]] is a 2 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=1SG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SG0 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1sg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg0 OCA], [https://pdbe.org/1sg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1sg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>
== 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/sg/1sg0_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=1sg0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SG0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, FAD and STL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SG0 OCA].
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of quinone reductase 2 in complex with resveratrol., Buryanovskyy L, Fu Y, Boyd M, Ma Y, Hsieh TC, Wu JM, Zhang Z, Biochemistry. 2004 Sep 14;43(36):11417-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15350128 15350128]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: NAD(P)H dehydrogenase (quinone)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Boyd M]]
[[Category: Boyd, M.]]
[[Category: Buryanovskyy L]]
[[Category: Buryanovskyy, L.]]
[[Category: Fu Y]]
[[Category: Fu, Y.]]
[[Category: Ma Y]]
[[Category: Ma, Y.]]
[[Category: Tsieh TC]]
[[Category: Tsieh, T.C.]]
[[Category: Wu JM]]
[[Category: Wu, J.M.]]
[[Category: Zhang Z]]
[[Category: Zhang, Z.]]
[[Category: FAD]]
[[Category: STL]]
[[Category: ZN]]
[[Category: quinone reductase 2]]
[[Category: resveratrol]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:13:06 2007''

Latest revision as of 08:30, 14 February 2024

Crystal structure analysis of QR2 in complex with resveratrol

1sg0, resolution 1.50Å

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