3apo
From Proteopedia
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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=3apo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3apo RCSB], [http://www.ebi.ac.uk/pdbsum/3apo 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=3apo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3apo RCSB], [http://www.ebi.ac.uk/pdbsum/3apo PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 23:18, 24 December 2014
Crystal structure of full-length ERdj5
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