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2cfy
From Proteopedia
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| - | [[Image:2cfy.gif|left|200px]]<br /> | ||
| - | <applet load="2cfy" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cfy, resolution 2.70Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF HUMAN THIOREDOXIN REDUCTASE 1'''<br /> | ||
| - | == | + | ==Crystal structure of human thioredoxin reductase 1== |
| - | + | <StructureSection load='2cfy' size='340' side='right'caption='[[2cfy]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <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> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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> |
| - | [ | + | <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> | |
| - | [ | + | == Function == |
| - | [ | + | [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 == | |
| - | [ | + | [[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/cf/2cfy_consurf.spt"</scriptWhenChecked> |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2cfy ConSurf]. |
| - | + | <div style="clear:both"></div> | |
| - | + | ==See Also== | |
| + | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith C]] | ||
| + | [[Category: Debreczeni JE]] | ||
| + | [[Category: Edwards A]] | ||
| + | [[Category: Johansson C]] | ||
| + | [[Category: Kavanagh K]] | ||
| + | [[Category: Oppermann U]] | ||
| + | [[Category: Savitsky P]] | ||
| + | [[Category: Sundstrom M]] | ||
| + | [[Category: Weigelt J]] | ||
| + | [[Category: Von Delft F]] | ||
Current revision
Crystal structure of human thioredoxin reductase 1
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