3apo

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==Crystal structure of full-length ERdj5==
==Crystal structure of full-length ERdj5==
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<StructureSection load='3apo' size='340' side='right' caption='[[3apo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3apo' size='340' side='right'caption='[[3apo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3apo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3apo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APO FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3apq|3apq]], [[3aps|3aps]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3apq|3apq]], [[3aps|3aps]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJC10, ERDJ5, JPDI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJC10, ERDJ5, JPDI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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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://pdbe.org/3apo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3apo RCSB], [http://www.ebi.ac.uk/pdbsum/3apo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3apo ProSAT]</span></td></tr>
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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=3apo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apo OCA], [https://pdbe.org/3apo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3apo RCSB], [https://www.ebi.ac.uk/pdbsum/3apo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3apo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[[https://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 ==
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==See Also==
==See Also==
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*[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
*[[ER-resident protein|ER-resident protein]]
*[[ER-resident protein|ER-resident protein]]
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*[[Molecular Playground/ERDj5|Molecular Playground/ERDj5]]
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Lk3 transgenic mice]]
[[Category: Inaba, K]]
[[Category: Inaba, K]]

Revision as of 15:00, 29 December 2021

Crystal structure of full-length ERdj5

PDB ID 3apo

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