1wou

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{{Seed}}
 
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[[Image:1wou.png|left|200px]]
 
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==Crystal Structure of human Trp14==
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The line below this paragraph, containing "STRUCTURE_1wou", creates the "Structure Box" on the page.
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<StructureSection load='1wou' size='340' side='right'caption='[[1wou]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1wou]] is a 1 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=1WOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOU 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]] 1.8&#8491;</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=1wou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wou OCA], [https://pdbe.org/1wou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wou RCSB], [https://www.ebi.ac.uk/pdbsum/1wou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wou ProSAT]</span></td></tr>
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{{STRUCTURE_1wou| PDB=1wou | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TXD17_HUMAN TXD17_HUMAN] Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.<ref>PMID:14607844</ref> <ref>PMID:14607843</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/wo/1wou_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=1wou 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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Thioredoxin-related protein 14 (TRP14) is involved in regulating tumor necrosis factor-alpha-induced signaling pathways in a different manner from human thioredoxin 1 (Trx1). Here, we report the crystal structure of human TRP14 determined at 1.8-A resolutions. The structure reveals a typical thioredoxin fold with characteristic structural features that account for the substrate specificity of the protein. The surface of TRP14 in the vicinity of the active site includes an extended loop and an additional alpha-helix, and the distribution of charged residues in the surface is different from Trx1. The distinctive dipeptide between the redox-active cysteines contributes to stabilizing the thiolate anion of the active site cysteine 43, increasing reactivity of the cysteine toward substrates. These structural differences in the active site suggest that TRP14 has evolved to regulate cellular redox signaling by recognizing a distinctive group of substrates that would complement the group of proteins regulated by Trx1.
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===Crystal Structure of human Trp14===
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Structural basis of cellular redox regulation by human TRP14.,Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:15355959<ref>PMID:15355959</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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The line below this paragraph, {{ABSTRACT_PUBMED_15355959}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1wou" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15355959 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15355959}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1WOU is a [[Single protein]] structure of sequence 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=1WOU OCA].
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==Reference==
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Structural basis of cellular redox regulation by human TRP14., Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE, J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15355959 15355959]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cho, Y H.]]
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[[Category: Cho YH]]
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[[Category: Chung, Y J.]]
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[[Category: Chung YJ]]
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[[Category: Jeong, W.]]
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[[Category: Jeong W]]
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[[Category: Kim, S J.]]
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[[Category: Kim SJ]]
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[[Category: Lee, S C.]]
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[[Category: Lee SC]]
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[[Category: Rhee, S G.]]
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[[Category: Rhee SG]]
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[[Category: Ryu, S E.]]
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[[Category: Ryu SE]]
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[[Category: Woo, J R.]]
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[[Category: Woo JR]]
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[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:09:40 2008''
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Current revision

Crystal Structure of human Trp14

PDB ID 1wou

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