3aps - Revision history

OCA at 15:51, 4 October 2023

2023-10-04T15:51:40Z

← Older revision		Revision as of 15:51, 4 October 2023
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	<StructureSection load='3aps' size='340' side='right'caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3aps' size='340' side='right'caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3aps]] is a 2 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=3APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APS FirstGlance]. <br>		<table><tr><td colspan='2'>[[3aps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APS FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3apo\|3apo]], [[3apq\|3apq]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	~~<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>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [https://pdbe.org/3aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [https://www.ebi.ac.uk/pdbsum/3aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aps ProSAT]</span></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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [https://pdbe.org/3aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [https://www.ebi.ac.uk/pdbsum/3aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aps ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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>		[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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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Inaba, K]]		[[Category: Inaba K]]
	[[Category: Nagata, K]]		[[Category: Nagata K]]
	[[Category: Suzuki, M]]		[[Category: Suzuki M]]
	~~[[Category: Cxxc motif]]~~
	~~[[Category: Endoplasmic reticulum]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Thioredoxin fold~~]]

OCA at 15:00, 29 December 2021

2021-12-29T15:00:30Z

← Older revision		Revision as of 15:00, 29 December 2021
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	==Crystal structure of Trx4 domain of ERdj5==		==Crystal structure of Trx4 domain of ERdj5==
	<StructureSection load='3aps' size='340' side='right' caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3aps' size='340' side='right'caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3aps]] is a 2 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=3APS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3APS FirstGlance]. <br>		<table><tr><td colspan='2'>[[3aps]] is a 2 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=3APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3apo\|3apo]], [[3apq\|3apq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3apo\|3apo]], [[3apq\|3apq]]</div></td></tr>
	<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>		<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>
	<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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [~~http~~://pdbe.org/3aps PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3aps PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3aps ProSAT]</span></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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [https://pdbe.org/3aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [https://www.ebi.ac.uk/pdbsum/3aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aps ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>		[[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==
			*[[DnaJ homolog 3D structures\|DnaJ homolog 3D structures]]
	*[[ER-resident protein\|ER-resident protein]]		*[[ER-resident protein\|ER-resident protein]]
	== References ==		== References ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Inaba, K]]		[[Category: Inaba, K]]

OCA at 22:51, 5 August 2016

2016-08-05T22:51:09Z

← Older revision		Revision as of 22:51, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of Trx4 domain of ERdj5==		==Crystal structure of Trx4 domain of ERdj5==
	<StructureSection load='3aps' size='340' side='right' caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3aps' size='340' side='right' caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3aps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APS FirstGlance]. <br>		<table><tr><td colspan='2'>[[3aps]] is a 2 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=3APS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3apo\|3apo]], [[3apq\|3apq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3apo\|3apo]], [[3apq\|3apq]]</td></tr>
	<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 ~~Mus musculus~~])</td></tr>		<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>
	<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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [http://www.ebi.ac.uk/pdbsum/3aps 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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [http://pdbe.org/3aps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [http://www.ebi.ac.uk/pdbsum/3aps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aps ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 3aps" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Inaba, K]]		[[Category: Inaba, K]]
	[[Category: Nagata, K]]		[[Category: Nagata, K]]

OCA at 22:37, 25 December 2014

2014-12-25T22:37:29Z

← Older revision		Revision as of 22:37, 25 December 2014
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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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [http://www.ebi.ac.uk/pdbsum/3aps 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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [http://www.ebi.ac.uk/pdbsum/3aps 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 ==

OCA at 10:29, 3 December 2014

2014-12-03T10:29:56Z

← Older revision		Revision as of 10:29, 3 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~3aps~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of Trx4 domain of ERdj5==
			<StructureSection load='3aps' size='340' side='right' caption='[[3aps]], [[Resolution\|resolution]] 1.90Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3aps]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APS FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3apo\|3apo]], [[3apq\|3apq]]</td></tr>
			<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 Mus musculus])</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=3aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aps OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aps RCSB], [http://www.ebi.ac.uk/pdbsum/3aps PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			ER-associated degradation (ERAD) is an ER quality-control process that eliminates terminally misfolded proteins. ERdj5 was recently discovered to be a key ER-resident PDI family member protein that accelerates ERAD by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. We here solved the crystal structure of full-length ERdj5, thereby revealing that ERdj5 contains the N-terminal J domain and six tandem thioredoxin domains that can be divided into the N- and C-terminal clusters. Our systematic biochemical analyses indicated that two thioredoxin domains that constitute the C-terminal cluster form the highly reducing platform that interacts with EDEM1 and reduces EDEM1-recruited substrates, leading to their facilitated degradation. The pulse-chase experiment further provided direct evidence for the sequential movement of an ERAD substrate from calnexin to the downstream EDEM1-ERdj5 complex, and then to the retrotranslocation channel, probably through BiP. We present a detailed molecular view of how ERdj5 mediates ERAD in concert with EDEM1.

	~~{{STRUCTURE_3aps\| PDB=3aps \| SCENE= }}~~		Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5.,Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K Mol Cell. 2011 Feb 18;41(4):432-44. PMID:21329881<ref>PMID:21329881</ref>

	~~===Crystal structure~~ of ~~Trx4 domain~~ of ~~ERdj5===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_21329881}}~~		==See Also==
			*[[ER-resident protein\|ER-resident protein]]
	==~~About this Structure~~==		== References ==
	[[~~3aps~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APS OCA].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:021329881<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Inaba, K.]]		[[Category: Inaba, K]]
	[[Category: Nagata, K.]]		[[Category: Nagata, K]]
	[[Category: Suzuki, M.]]		[[Category: Suzuki, M]]
	[[Category: Cxxc motif]]		[[Category: Cxxc motif]]
	[[Category: Endoplasmic reticulum]]		[[Category: Endoplasmic reticulum]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Thioredoxin fold]]		[[Category: Thioredoxin fold]]

OCA at 15:47, 27 February 2013

2013-02-27T15:47:06Z

← Older revision		Revision as of 15:47, 27 February 2013
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	[[Image:3aps.~~jpg~~\|left\|200px]]		[[Image:3aps.png\|left\|200px]]

	~~<!--~~
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	{{STRUCTURE_3aps\| PDB=3aps \| SCENE= }}		{{STRUCTURE_3aps\| PDB=3aps \| SCENE= }}

	===Crystal structure of Trx4 domain of ERdj5===		===Crystal structure of Trx4 domain of ERdj5===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_21329881}}, adds the Publication Abstract to the page~~
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	==Reference==		==Reference==
	<ref group="xtra">PMID:~~21329881~~</ref><references group="xtra"/>		<ref group="xtra">PMID:021329881</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Inaba, K.]]		[[Category: Inaba, K.]]
	[[Category: Nagata, K.]]		[[Category: Nagata, K.]]
	[[Category: Suzuki, M.]]		[[Category: Suzuki, M.]]
			[[Category: Cxxc motif]]
			[[Category: Endoplasmic reticulum]]
			[[Category: Oxidoreductase]]
			[[Category: Thioredoxin fold]]

OCA: Protected "3aps" [edit=sysop:move=sysop]

2011-04-21T10:43:30Z

Protected "3aps" [edit=sysop:move=sysop]

← Older revision	Revision as of 10:43, 21 April 2011
(No difference)

OCA at 10:43, 21 April 2011

2011-04-21T10:43:26Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3aps.jpg|left|200px]]
-The entry 3aps is ON HOLD  until Paper Publication
+<!--
-Authors: Inaba, K., Suzuki, M., Nagata, K.
+===Crystal structure of Trx4 domain of ERdj5===
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec  8 11:26:24 2010''
+<!--

OCA at 08:14, 8 December 2010

2010-12-08T08:14:21Z

← Older revision		Revision as of 08:14, 8 December 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3aps is ON HOLD		The entry 3aps is ON HOLD until Paper Publication

	Authors: Inaba, K., Suzuki, M., Nagata, K.		Authors: Inaba, K., Suzuki, M., Nagata, K.
Line 7:		Line 7:
	Description: Crystal structure of Trx4 domain of ERdj5		Description: Crystal structure of Trx4 domain of ERdj5

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Nov~~ ~~3 09~~:58:34 2010''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:26:24 2010''

OCA: New page: '''Unreleased structure''' The entry 3aps is ON HOLD Authors: Inaba, K., Suzuki, M., Nagata, K. Description: Crystal structure of Trx4 domain of ERdj5 ''Page seeded by [http://oca.wei...

2010-11-03T06:47:55Z

New page: '''Unreleased structure''' The entry 3aps is ON HOLD Authors: Inaba, K., Suzuki, M., Nagata, K. Description: Crystal structure of Trx4 domain of ERdj5 ''Page seeded by [http://oca.wei...

New page

'''Unreleased structure'''

The entry 3aps is ON HOLD

Authors: Inaba, K., Suzuki, M., Nagata, K.

Description: Crystal structure of Trx4 domain of ERdj5

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 3 09:58:34 2010''