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1x5c
From Proteopedia
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| - | [[Image:1x5c.gif|left|200px]]<br /><applet load="1x5c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1x5c" /> | ||
| - | '''The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase'''<br /> | ||
| - | == | + | ==The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase== |
| - | + | <StructureSection load='1x5c' size='340' side='right'caption='[[1x5c]]' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1x5c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X5C FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1x5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x5c OCA], [https://pdbe.org/1x5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x5c RCSB], [https://www.ebi.ac.uk/pdbsum/1x5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x5c ProSAT], [https://www.topsan.org/Proteins/RSGI/1x5c TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</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/x5/1x5c_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1x5c ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Inoue M]] | |
| - | [[Category: Inoue | + | [[Category: Kigawa T]] |
| - | [[Category: Kigawa | + | [[Category: Koshiba S]] |
| - | [[Category: Koshiba | + | [[Category: Tochio N]] |
| - | + | [[Category: Yokoyama S]] | |
| - | [[Category: Tochio | + | |
| - | [[Category: Yokoyama | + | |
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Current revision
The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase
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Categories: Homo sapiens | Large Structures | Inoue M | Kigawa T | Koshiba S | Tochio N | Yokoyama S
