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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 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN THIOREDOXIN REDUCTASE 1'''<br />


==About this Structure==
==Crystal structure of human thioredoxin reductase 1==
2CFY 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 FAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFY OCA]].
<StructureSection load='2cfy' size='340' side='right'caption='[[2cfy]], [[Resolution|resolution]] 2.70&Aring;' 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]] 2.7&#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></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: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Thioredoxin-disulfide reductase]]
[[Category: Arrowsmith C]]
[[Category: Arrowsmith, C.]]
[[Category: Debreczeni JE]]
[[Category: Debreczeni, J.E.]]
[[Category: Edwards A]]
[[Category: Delft, F.Von.]]
[[Category: Johansson C]]
[[Category: Edwards, A.]]
[[Category: Kavanagh K]]
[[Category: Johansson, C.]]
[[Category: Oppermann U]]
[[Category: Kavanagh, K.]]
[[Category: Savitsky P]]
[[Category: Oppermann, U.]]
[[Category: Sundstrom M]]
[[Category: Savitsky, P.]]
[[Category: Weigelt J]]
[[Category: Sundstrom, M.]]
[[Category: Von Delft F]]
[[Category: Weigelt, J.]]
[[Category: FAD]]
[[Category: nadp]]
[[Category: oxidoreductase]]
[[Category: phosphorylation]]
[[Category: redox-active center]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:36:20 2007''

Latest revision as of 12:03, 6 November 2024

Crystal structure of human thioredoxin reductase 1Crystal structure of human thioredoxin reductase 1

Structural highlights

2cfy is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Hofmann ER, Boyanapalli M, Lindner DJ, Weihua X, Hassel BA, Jagus R, Gutierrez PL, Kalvakolanu DV. Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid. Mol Cell Biol. 1998 Nov;18(11):6493-504. PMID:9774665
  2. ↑ Tamura T, Stadtman TC. A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1006-11. PMID:8577704
  3. ↑ Damdimopoulos AE, Miranda-Vizuete A, Treuter E, Gustafsson JA, Spyrou G. An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling. J Biol Chem. 2004 Sep 10;279(37):38721-9. Epub 2004 Jun 14. PMID:15199063 doi:http://dx.doi.org/10.1074/jbc.M402753200
  4. ↑ Dammeyer P, Damdimopoulos AE, Nordman T, Jimenez A, Miranda-Vizuete A, Arner ES. Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1. J Biol Chem. 2008 Feb 1;283(5):2814-21. Epub 2007 Nov 27. PMID:18042542 doi:http://dx.doi.org/10.1074/jbc.M708939200

2cfy, resolution 2.70Å

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