1x5c
From Proteopedia
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==The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase== | ==The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase== | ||
| - | <StructureSection load='1x5c' size='340' side='right' caption='[[1x5c | + | <StructureSection load='1x5c' size='340' side='right'caption='[[1x5c]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1x5c]] is a 1 chain structure with sequence from [ | + | <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=' | + | </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> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Inoue | + | [[Category: Inoue M]] |
| - | [[Category: Kigawa | + | [[Category: Kigawa T]] |
| - | [[Category: Koshiba | + | [[Category: Koshiba S]] |
| - | + | [[Category: Tochio N]] | |
| - | [[Category: Tochio | + | [[Category: Yokoyama S]] |
| - | [[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
