6u3r - Revision history

OCA at 11:04, 14 June 2023

OCA — Wed, 14 Jun 2023 11:04:32 GMT

←Older revision		Revision as of 11:04, 14 June 2023
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	==Solution NMR structure of the DNAJB6b deltaST variant (Aligned on the J domain)==		==Solution NMR structure of the DNAJB6b deltaST variant (Aligned on the J domain)==
-	<StructureSection load='6u3r' size='340' side='right'caption='[[6u3r~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='6u3r' size='340' side='right'caption='[[6u3r]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6u3r]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U3R OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6U3R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6u3r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U3R FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNAJB6, HSJ2, MRJ, MSJ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</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=6u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u3r OCA], [https://pdbe.org/6u3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u3r RCSB], [https://www.ebi.ac.uk/pdbsum/6u3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u3r ProSAT]</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=6u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u3r OCA], [~~http~~://pdbe.org/6u3r PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6u3r RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6u3r PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6u3r ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Autosomal dominant limb-girdle muscular dystrophy type 1D. The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786).<ref>PMID:22366786</ref>	+	[https://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN] Autosomal dominant limb-girdle muscular dystrophy type 1D. The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786).<ref>PMID:22366786</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref>	+	[https://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 6u3r" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6u3r" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[DnaJ homolog 3D structures\|DnaJ homolog 3D structures]]
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Clore~~, G M~~]]	+	[[Category: Clore GM]]
-	[[Category: Karamanos~~, T K]]~~	+	[[Category: Karamanos TK]]
-	~~[[Category: Amyloid]]~~	+
-	~~[[Category: Anti-aggregation]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Hsp40~~]]	+

OCA at 08:16, 23 October 2019

OCA — Wed, 23 Oct 2019 08:16:41 GMT

←Older revision		Revision as of 08:16, 23 October 2019
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	<StructureSection load='6u3r' size='340' side='right'caption='[[6u3r]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='6u3r' size='340' side='right'caption='[[6u3r]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6u3r]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U3R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6u3r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U3R FirstGlance]. <br>
-	</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=6u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u3r OCA], [http://pdbe.org/6u3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u3r RCSB], [http://www.ebi.ac.uk/pdbsum/6u3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u3r ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNAJB6, HSJ2, MRJ, MSJ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u3r OCA], [http://pdbe.org/6u3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u3r RCSB], [http://www.ebi.ac.uk/pdbsum/6u3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u3r ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref>		[[http://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	J-domain chaperones are involved in the efficient handover of misfolded/partially folded proteins to Hsp70 but also function independently to protect against cell death. Due to their high flexibility, the mechanism by which they regulate the Hsp70 cycle and how specific substrate recognition is performed remains unknown. Here we focus on DNAJB6b, which has been implicated in various human diseases and represents a key player in protection against neurodegeneration and protein aggregation. Using a variant that exists mainly in a monomeric form, we report the solution structure of an Hsp40 containing not only the J and C-terminal substrate binding (CTD) domains but also the functionally important linkers. The structure reveals a highly dynamic protein in which part of the linker region masks the Hsp70 binding site. Transient interdomain interactions via regions crucial for Hsp70 binding create a closed, autoinhibited state and help retain the monomeric form of the protein. Detailed NMR analysis shows that the CTD (but not the J domain) self-associates to form an oligomer comprising approximately 35 monomeric units, revealing an intricate balance between intramolecular and intermolecular interactions. The results shed light on the mechanism of autoregulation of the Hsp70 cycle via conserved parts of the linker region and reveal the mechanism of DNAJB6b oligomerization and potentially antiaggregation.
		+
		+	Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis.,Karamanos TK, Tugarinov V, Clore GM Proc Natl Acad Sci U S A. 2019 Oct 7. pii: 1914999116. doi:, 10.1073/pnas.1914999116. PMID:31591220<ref>PMID:31591220</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6u3r" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Clore, G M]]		[[Category: Clore, G M]]

OCA at 05:28, 10 October 2019

OCA — Thu, 10 Oct 2019 05:28:53 GMT

←Older revision		Revision as of 05:28, 10 October 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~6u3r~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Solution NMR structure of the DNAJB6b deltaST variant (Aligned on the J domain)==
-		+	<StructureSection load='6u3r' size='340' side='right'caption='[[6u3r]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6u3r]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U3R FirstGlance]. <br>
-	~~Description:~~	+	</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=6u3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u3r OCA], [http://pdbe.org/6u3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u3r RCSB], [http://www.ebi.ac.uk/pdbsum/6u3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u3r ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Autosomal dominant limb-girdle muscular dystrophy type 1D. The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786).<ref>PMID:22366786</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN]] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Clore, G M]]
		+	[[Category: Karamanos, T K]]
		+	[[Category: Amyloid]]
		+	[[Category: Anti-aggregation]]
		+	[[Category: Chaperone]]
		+	[[Category: Hsp40]]

OCA at 08:09, 2 October 2019

OCA — Wed, 02 Oct 2019 08:09:38 GMT

←Older revision		Revision as of 08:09, 2 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6u3r is ON HOLD	+	The entry 6u3r is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6u3r" [edit=sysop:move=sysop]

OCA — Wed, 28 Aug 2019 14:07:10 GMT

Protected "6u3r" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:07, 28 August 2019

OCA: New page: '''Unreleased structure''' The entry 6u3r is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 28 Aug 2019 14:07:08 GMT

New page: '''Unreleased structure''' The entry 6u3r is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6u3r is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]