5xir - Revision history

OCA at 10:30, 14 June 2023

2023-06-14T10:30:49Z

←Older revision		Revision as of 10:30, 14 June 2023
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	==Solution structure for human HSP70 substrate binding domain L542Y mutant==		==Solution structure for human HSP70 substrate binding domain L542Y mutant==
-	<StructureSection load='5xir' size='340' side='right'caption='[[5xir~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='5xir' size='340' side='right'caption='[[5xir]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xir]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XIR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5XIR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xir]] 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=5XIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XIR FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xi9\|5xi9]]</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=5xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xir OCA], [https://pdbe.org/5xir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xir RCSB], [https://www.ebi.ac.uk/pdbsum/5xir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xir ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xir OCA], [~~http~~://pdbe.org/5xir PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xir RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xir PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xir ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>	+	[https://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hoshikawa, M]]	+	[[Category: Hoshikawa M]]
-	[[Category: Tate, S]]	+	[[Category: Tate S]]
-	[[Category: Tochio, N]]	+	[[Category: Tochio N]]
-	~~[[Category: Apo state]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Heat shock protein 70 kda~~]]	+

OCA at 06:51, 14 October 2020

2020-10-14T06:51:09Z

←Older revision		Revision as of 06:51, 14 October 2020
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	==Solution structure for human HSP70 substrate binding domain L542Y mutant==		==Solution structure for human HSP70 substrate binding domain L542Y mutant==
-	<StructureSection load='5xir' size='340' side='right' caption='[[5xir]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='5xir' size='340' side='right'caption='[[5xir]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xir]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XIR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XIR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xir]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XIR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XIR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xi9\|5xi9]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xi9\|5xi9]]</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=5xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xir OCA], [http://pdbe.org/5xir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xir RCSB], [http://www.ebi.ac.uk/pdbsum/5xir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xir ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xir OCA], [http://pdbe.org/5xir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xir RCSB], [http://www.ebi.ac.uk/pdbsum/5xir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xir ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 5xir" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5xir" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Hoshikawa, M]]		[[Category: Hoshikawa, M]]
	[[Category: Tate, S]]		[[Category: Tate, S]]

OCA at 05:25, 16 May 2018

2018-05-16T05:25:00Z

←Older revision		Revision as of 05:25, 16 May 2018
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-	'''Unreleased structure'''

-	~~The entry~~ 5xir is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Solution structure for human HSP70 substrate binding domain L542Y mutant==
		+	<StructureSection load='5xir' size='340' side='right' caption='[[5xir]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5xir]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XIR FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xi9\|5xi9]]</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=5xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xir OCA], [http://pdbe.org/5xir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xir RCSB], [http://www.ebi.ac.uk/pdbsum/5xir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xir ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The stress-induced 70 kDa heat shock protein (Hsp70) functions as a molecular chaperone to maintain protein homeostasis. Hsp70 contains an N-terminal ATPase domain (NBD) and a C-terminal substrate-binding domain (SBD). The SBD is divided into the beta subdomain containing the substrate-binding site (betaSBD) and the alpha-helical subdomain (alphaLid) that covers the betaSBD. In this report, the solution structures of two different forms of the SBD from human Hsp70 were solved. One structure shows the alphaLid bound to the substrate-binding site intramolecularly, whereas this intramolecular binding mode is absent in the other structure solved. Structural comparison of the two SBDs from Hsp70 revealed that client-peptide binding rearranges residues at the interdomain contact site, which impairs interdomain contact between the SBD and the NBD. Peptide binding also disrupted the inter-subdomain interaction connecting the alphaLid to the betaSBD, which allows the binding of the alphaLid to the NBD. The results provide a mechanism for interdomain communication upon substrate binding from the SBD to the NBD via the lynchpin site in the betaSBD of human Hsp70. In comparison to the bacterial ortholog, DnaK, some remarkable differences in the allosteric signal propagation among residues within the Hsp70 SBD exist.

-	~~Authors: Hoshikawa~~, M., Tochio, N., Tate, S.	+	Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication.,Umehara K, Hoshikawa M, Tochio N, Tate SI Molecules. 2018 Feb 27;23(3). pii: molecules23030528. doi:, 10.3390/molecules23030528. PMID:29495458<ref>PMID:29495458</ref>

-	~~Description: Solution structure for human HSP70 substrate binding domain L542Y mutant~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5xir" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Hoshikawa, M]]		[[Category: Hoshikawa, M]]
	[[Category: Tate, S]]		[[Category: Tate, S]]
	[[Category: Tochio, N]]		[[Category: Tochio, N]]
		+	[[Category: Apo state]]
		+	[[Category: Chaperone]]
		+	[[Category: Heat shock protein 70 kda]]

OCA at 15:30, 27 September 2017

2017-09-27T15:30:06Z

←Older revision		Revision as of 15:30, 27 September 2017
Line 7:		Line 7:
	Description: Solution structure for human HSP70 substrate binding domain L542Y mutant		Description: Solution structure for human HSP70 substrate binding domain L542Y mutant
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Tate, S]]
	[[Category: Hoshikawa, M]]		[[Category: Hoshikawa, M]]
		+	[[Category: Tate, S]]
	[[Category: Tochio, N]]		[[Category: Tochio, N]]

OCA at 14:51, 17 May 2017

2017-05-17T14:51:05Z

←Older revision		Revision as of 14:51, 17 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5xir is ON HOLD	+	The entry 5xir is ON HOLD until Paper Publication

	Authors: Hoshikawa, M., Tochio, N., Tate, S.		Authors: Hoshikawa, M., Tochio, N., Tate, S.

OCA: Protected "5xir" [edit=sysop:move=sysop]

2017-05-04T12:14:50Z

Protected "5xir" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:14, 4 May 2017

OCA: New page: '''Unreleased structure''' The entry 5xir is ON HOLD Authors: Hoshikawa, M., Tochio, N., Tate, S. Description: Solution structure for human HSP70 substrate binding domain L542Y mutant ...

2017-05-04T12:14:48Z

New page: '''Unreleased structure''' The entry 5xir is ON HOLD Authors: Hoshikawa, M., Tochio, N., Tate, S. Description: Solution structure for human HSP70 substrate binding domain L542Y mutant ...

New page

'''Unreleased structure'''

The entry 5xir is ON HOLD

Authors: Hoshikawa, M., Tochio, N., Tate, S.

Description: Solution structure for human HSP70 substrate binding domain L542Y mutant
[[Category: Unreleased Structures]]
[[Category: Tate, S]]
[[Category: Hoshikawa, M]]
[[Category: Tochio, N]]