1bjx

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{{Seed}}
 
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[[Image:1bjx.png|left|200px]]
 
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==HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1bjx", creates the "Structure Box" on the page.
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<StructureSection load='1bjx' size='340' side='right'caption='[[1bjx]]' 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'>[[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>
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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">Solution NMR</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=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>
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{{STRUCTURE_1bjx| PDB=1bjx | SCENE= }}
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</table>
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== Function ==
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[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>
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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/bj/1bjx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1bjx 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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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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===HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES===
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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&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_10383197}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1bjx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10383197 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10383197}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1BJX is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10383197 10383197]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein disulfide-isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Darby NJ]]
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[[Category: Darby, N J.]]
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[[Category: Dijkstra K]]
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[[Category: Dijkstra, K.]]
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[[Category: Kemmink J]]
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[[Category: Kemmink, J.]]
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[[Category: Mariani M]]
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[[Category: Mariani, M.]]
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[[Category: Nilges M]]
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[[Category: Nilges, M.]]
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[[Category: Penka E]]
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[[Category: Penka, E.]]
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[[Category: Scheek RM]]
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[[Category: Scheek, R M.]]
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[[Category: Electron transport]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Isomerase]]
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[[Category: Redox-active center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:17:03 2008''
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Current revision

HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES

PDB ID 1bjx

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