2j3n

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{{Seed}}
 
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[[Image:2j3n.png|left|200px]]
 
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==X-ray structure of human thioredoxin reductase 1==
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The line below this paragraph, containing "STRUCTURE_2j3n", creates the "Structure Box" on the page.
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<StructureSection load='2j3n' size='340' side='right'caption='[[2j3n]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2j3n]] 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=2J3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.8&#8491;</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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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{{STRUCTURE_2j3n| PDB=2j3n | SCENE= }}
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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=2j3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3n OCA], [https://pdbe.org/2j3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3n RCSB], [https://www.ebi.ac.uk/pdbsum/2j3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3n ProSAT]</span></td></tr>
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</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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/2j3n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2j3n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulation of cellular redox reactions, growth and differentiation. The enzyme contains a selenocysteine residue at its C-terminal active site that is essential for catalysis. This redox center is located on a flexible arm, solvent-exposed and reactive towards electrophilic inhibitors, thus representing a target for antitumor drug development. During catalysis reducing equivalents are transferred from the cofactor NADPH to FAD, then to the N-terminal active site cysteine residues and from there to the flexible C-terminal part of the other subunit to be finally delivered to a variety of second substrates at the molecule's surface. Here we report the first crystal structure of hTrxR1 (Sec--&gt;Cys) in complex with FAD and NADP(+) at a resolution of 2.8 A. From the crystals three different conformations of the carboxy-terminal arm could be deduced. The predicted movement of the arm is facilitated by the concerted action of the three side-chain residues of N418, N419 and W407, which act as a guiding bar for the C-terminal sliding process. As supported by previous kinetic data, the three visualized conformations might reflect different stages in enzymatic catalysis. Comparison with other disulfide reductases including human glutathione reductase revealed specific inhibitor binding sites in the intersubunit cavity of hTrxR that can be exploited for structure-based inhibitor development.
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===X-RAY STRUCTURE OF HUMAN THIOREDOXIN REDUCTASE 1===
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The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis.,Fritz-Wolf K, Urig S, Becker K J Mol Biol. 2007 Jun 29;370(1):116-27. Epub 2007 Apr 24. PMID:17512005<ref>PMID:17512005</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j3n" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17512005}}, adds the Publication Abstract to the page
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*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17512005 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17512005}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2J3N is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3N OCA].
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==Reference==
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<ref group="xtra">PMID:17512005</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Thioredoxin-disulfide reductase]]
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[[Category: Large Structures]]
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[[Category: Becker, K.]]
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[[Category: Becker K]]
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[[Category: Fritz-Wolf, K.]]
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[[Category: Fritz-Wolf K]]
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[[Category: Urig, S.]]
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[[Category: Urig S]]
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[[Category: Cytoplasm]]
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[[Category: Electron transport]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Human]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphorylation]]
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[[Category: Pyridine nucleotide dependent disulfide reductase]]
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[[Category: Redox regulation]]
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[[Category: Redox-active center]]
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[[Category: Selenium]]
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[[Category: Selenocysteine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:40:49 2009''
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Current revision

X-ray structure of human thioredoxin reductase 1

PDB ID 2j3n

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