3uem: Difference between revisions
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New page: '''Unreleased structure''' The entry 3uem is ON HOLD Authors: Yu, Jiang, Wang, Chao, Huo, Lin, Feng, Wei, Wang, Chih-chen Description: Crystal structure of human PDI bb'a' domains |
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==Crystal structure of human PDI bb'a' domains== | |||
<StructureSection load='3uem' size='340' side='right'caption='[[3uem]], [[Resolution|resolution]] 2.29Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== 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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Feng W]] | |||
[[Category: Huo L]] | |||
[[Category: Wang C]] | |||
[[Category: Wang C-C]] | |||
[[Category: Yu J]] | |||
Latest revision as of 08:38, 20 March 2024
Crystal structure of human PDI bb'a' domains
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