4el1: Difference between revisions

</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=4el1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4el1 OCA], [https://pdbe.org/4el1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4el1 RCSB], [https://www.ebi.ac.uk/pdbsum/4el1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4el1 ProSAT]</span></td></tr>

[[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>