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2cfy

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Current revision (14:16, 13 December 2023) (edit) (undo)
 
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<StructureSection load='2cfy' size='340' side='right'caption='[[2cfy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2cfy' size='340' side='right'caption='[[2cfy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cfy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cfy]] is a 6 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=2CFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFY FirstGlance]. <br>
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</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></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">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w1c|1w1c]], [[1w1e|1w1e]]</div></td></tr>
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<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></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></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=2cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfy OCA], [https://pdbe.org/2cfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfy RCSB], [https://www.ebi.ac.uk/pdbsum/2cfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfy 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=2cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfy OCA], [https://pdbe.org/2cfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfy RCSB], [https://www.ebi.ac.uk/pdbsum/2cfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfy ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRXR1_HUMAN TRXR1_HUMAN] Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.<ref>PMID:9774665</ref> <ref>PMID:8577704</ref> <ref>PMID:15199063</ref> <ref>PMID:18042542</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
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== References ==
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<references/>
__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: Thioredoxin-disulfide reductase]]
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[[Category: Arrowsmith C]]
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[[Category: Arrowsmith, C]]
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[[Category: Debreczeni JE]]
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[[Category: Debreczeni, J E]]
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[[Category: Edwards A]]
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[[Category: Delft, F von]]
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[[Category: Johansson C]]
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[[Category: Edwards, A]]
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[[Category: Kavanagh K]]
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[[Category: Johansson, C]]
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[[Category: Oppermann U]]
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[[Category: Kavanagh, K]]
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[[Category: Savitsky P]]
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[[Category: Oppermann, U]]
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[[Category: Sundstrom M]]
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[[Category: Savitsky, P]]
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[[Category: Weigelt J]]
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[[Category: Sundstrom, M]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphorylation]]
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[[Category: Redox-active center]]
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Current revision

Crystal structure of human thioredoxin reductase 1

PDB ID 2cfy

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