3apq: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3apq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3apq RCSB], [http://www.ebi.ac.uk/pdbsum/3apq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3apq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3apq RCSB], [http://www.ebi.ac.uk/pdbsum/3apq PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/DJC10_MOUSE DJC10_MOUSE]] Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.<ref>PMID:12411443</ref> <ref>PMID:12446677</ref> <ref>PMID:18653895</ref> <ref>PMID:21329881</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||