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==PROTEIN DISULFIDE ISOMERASE==
==PROTEIN DISULFIDE ISOMERASE==
<StructureSection load='2bjx' size='340' side='right'caption='[[2bjx]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
<StructureSection load='2bjx' size='340' side='right'caption='[[2bjx]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bjx]] 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=2BJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJX FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
</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=2bjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjx OCA], [https://pdbe.org/2bjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjx RCSB], [https://www.ebi.ac.uk/pdbsum/2bjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjx ProSAT]</span></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=2bjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjx OCA], [https://pdbe.org/2bjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjx RCSB], [https://www.ebi.ac.uk/pdbsum/2bjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjx ProSAT]</span></td></tr>
</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>
[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: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein disulfide-isomerase]]
[[Category: Darby NJ]]
[[Category: Darby, N J]]
[[Category: Dijkstra K]]
[[Category: Dijkstra, K]]
[[Category: Kemmink J]]
[[Category: Kemmink, J]]
[[Category: Mariani M]]
[[Category: Mariani, M]]
[[Category: Nilges M]]
[[Category: Nilges, M]]
[[Category: Penka E]]
[[Category: Penka, E]]
[[Category: Scheek RM]]
[[Category: Scheek, R M]]
[[Category: Electron transport]]
[[Category: Endoplasmic reticulum]]
[[Category: Isomerase]]
[[Category: Redox-active center]]
Retrieved from "https://proteopedia.org/2bjx"