3uem

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{{STRUCTURE_3uem| PDB=3uem | SCENE= }}
 
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===Crystal structure of human PDI bb'a' domains===
 
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{{ABSTRACT_PUBMED_22090031}}
 
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==Function==
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==Crystal structure of human PDI bb'a' domains==
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[[http://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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<StructureSection load='3uem' size='340' side='right'caption='[[3uem]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3uem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UEM FirstGlance]. <br>
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[[3uem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene></td></tr>
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==Reference==
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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=3uem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uem OCA], [https://pdbe.org/3uem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uem RCSB], [https://www.ebi.ac.uk/pdbsum/3uem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uem ProSAT]</span></td></tr>
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<ref group="xtra">PMID:022090031</ref><references group="xtra"/><references/>
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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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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Feng, W.]]
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[[Category: Feng W]]
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[[Category: Huo, L.]]
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[[Category: Huo L]]
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[[Category: Wang, C.]]
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[[Category: Wang C]]
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[[Category: Wang, C C.]]
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[[Category: Wang C-C]]
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[[Category: Yu, J.]]
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[[Category: Yu J]]
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[[Category: Chaperone]]
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[[Category: Protein disulfide isomerase]]
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[[Category: Thioredoxin-like domain]]
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Current revision

Crystal structure of human PDI bb'a' domains

PDB ID 3uem

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