1bjx
From Proteopedia
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==HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES== | ==HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES== | ||
| - | <StructureSection load='1bjx' size='340' side='right'caption='[[1bjx | + | <StructureSection load='1bjx' size='340' side='right'caption='[[1bjx]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1bjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1bjx]] 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=1BJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BJX 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=1bjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjx OCA], [https://pdbe.org/1bjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjx RCSB], [https://www.ebi.ac.uk/pdbsum/1bjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjx 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=1bjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjx OCA], [https://pdbe.org/1bjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjx RCSB], [https://www.ebi.ac.uk/pdbsum/1bjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjx 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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1bjx ConSurf]. | </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=1bjx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Protein disulfide isomerase (PDI) is a multifunctional protein of the endoplasmic reticulum, which catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding. It consists of four domains designated a, b, b and a. Both a and a domains contains an active site with the sequence motif -Cys-Gly-His-Cys-involved directly in thiol-disulfide exchange reactions. As expected these domains have structures very similar to the ubiquitous redox protein thioredoxin. A low-resolution NMR structure of the b domain revealed that this domain adopts a fold similar to the PDI a domain and thioredoxin [Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. and Creighton, T.E. (1997) Curr. Biol. 7, 239-245]. A refined ensemble of solution structures based on the input of 1865 structural restraints shows that the structure of PDI b is well defined throughout the complete protein except for about 10 residues at the C-terminus of the sequence. 15N relaxation data show that these residues are disordered and not part of this structural domain. Therefore the domain boundaries of PDI can now be fixed with reasonable precision. Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity. | ||
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| - | The structure in solution of the b domain of protein disulfide isomerase.,Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ J Biomol NMR. 1999 Apr;13(4):357-68. PMID:10383197<ref>PMID:10383197</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1bjx" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Darby NJ]] | |
| - | [[Category: Darby | + | [[Category: Dijkstra K]] |
| - | [[Category: Dijkstra | + | [[Category: Kemmink J]] |
| - | [[Category: Kemmink | + | [[Category: Mariani M]] |
| - | [[Category: Mariani | + | [[Category: Nilges M]] |
| - | [[Category: Nilges | + | [[Category: Penka E]] |
| - | [[Category: Penka | + | [[Category: Scheek RM]] |
| - | [[Category: Scheek | + | |
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Revision as of 15:33, 13 March 2024
HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES
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Categories: Homo sapiens | Large Structures | Darby NJ | Dijkstra K | Kemmink J | Mariani M | Nilges M | Penka E | Scheek RM
