2cq9

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==Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA==
==Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA==
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<StructureSection load='2cq9' size='340' side='right'caption='[[2cq9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2cq9' size='340' side='right'caption='[[2cq9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CQ9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CQ9 FirstGlance]. <br>
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</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=2cq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cq9 OCA], [https://pdbe.org/2cq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cq9 RCSB], [https://www.ebi.ac.uk/pdbsum/2cq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cq9 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cq9 TOPSAN]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cq9 OCA], [https://pdbe.org/2cq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cq9 RCSB], [https://www.ebi.ac.uk/pdbsum/2cq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cq9 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cq9 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLRX2_HUMAN GLRX2_HUMAN]] Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.<ref>PMID:11297543</ref> <ref>PMID:14676218</ref> <ref>PMID:15328416</ref> <ref>PMID:15649413</ref>
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[https://www.uniprot.org/uniprot/GLRX2_HUMAN GLRX2_HUMAN] Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.<ref>PMID:11297543</ref> <ref>PMID:14676218</ref> <ref>PMID:15328416</ref> <ref>PMID:15649413</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/2cq9_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/2cq9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abe, T]]
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[[Category: Abe T]]
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[[Category: Hayashi, F]]
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[[Category: Hayashi F]]
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[[Category: Hirota, H]]
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[[Category: Hirota H]]
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[[Category: Structural genomic]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Glutaredoxin]]
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[[Category: Glutaredoxin 2]]
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[[Category: Glutathione-s-transferase]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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[[Category: Unknown function]]
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Current revision

Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA

PDB ID 2cq9

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