2e8a - Revision history

OCA at 08:36, 25 October 2023

2023-10-25T08:36:21Z

← Older revision		Revision as of 08:36, 25 October 2023
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	<StructureSection load='2e8a' size='340' side='right'caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2e8a' size='340' side='right'caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8A FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID~~-~~ADENYLATE+ESTER'>ANP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.77Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height~~: ~~3em;~~'>~~[[2e88\|2e88]]~~</~~div~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [https://pdbe.org/2e8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [https://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8a ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [https://pdbe.org/2e8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [https://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8a ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~HS71B_HUMAN HS71B_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: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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ishii, R]]		[[Category: Ishii R]]
	[[Category: Kishishita, S]]		[[Category: Kishishita S]]
	~~[[Category: Structural genomic~~]]		[[Category: Shida M]]
	[[Category: Shida, M]]		[[Category: Shirouzu M]]
	[[Category: Shirouzu, M]]		[[Category: Takagi T]]
	[[Category: Takagi, T]]		[[Category: Yokoyama S]]
	[[Category: Yokoyama, S]]
	~~[[Category: Anp]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: National project on protein structural and functional analyse]]~~
	~~[[Category: Nppsfa]]~~
	~~[[Category: Rsgi~~]]

OCA at 17:21, 15 December 2021

2021-12-15T17:21:43Z

← Older revision		Revision as of 17:21, 15 December 2021
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	<StructureSection load='2e8a' size='340' side='right'caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2e8a' size='340' side='right'caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2E8A FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2e88\|2e88]]</div></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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [~~http~~://pdbe.org/2e8a PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8a ProSAT], [~~http~~://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [https://pdbe.org/2e8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [https://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8a ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/HS71B_HUMAN HS71B_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:23973223</ref>		[[https://www.uniprot.org/uniprot/HS71B_HUMAN HS71B_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:23973223</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:29, 11 March 2020

2020-03-11T08:29:05Z

← Older revision		Revision as of 08:29, 11 March 2020
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	==Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP==		==Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP==
	<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2e8a' size='340' side='right'caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
Line 31:		Line 31:

	==See Also==		==See Also==
	*[[Heat Shock ~~Proteins~~\|Heat Shock ~~Proteins~~]]		*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Ishii, R]]		[[Category: Ishii, R]]
	[[Category: Kishishita, S]]		[[Category: Kishishita, S]]

OCA at 06:27, 6 June 2018

2018-06-06T06:27:46Z

← Older revision		Revision as of 06:27, 6 June 2018
Line 1:		Line 1:

	==Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP==		==Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP==
	<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://pdbe.org/2e8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://pdbe.org/2e8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8a ProSAT], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8a_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8a_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e8a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 10:23, 11 September 2015

2015-09-11T10:23:05Z

← Older revision		Revision as of 10:23, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://pdbe.org/2e8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HS71B_HUMAN HS71B_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:23973223</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 25:		Line 27:
	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 2e8a" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Ishii, R]]		[[Category: Ishii, R]]
	[[Category: Kishishita, S]]		[[Category: Kishishita, S]]

OCA at 15:08, 25 December 2014

2014-12-25T15:08:49Z

← Older revision		Revision as of 15:08, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</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=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ishii, R.]]		[[Category: Ishii, R]]
	[[Category: Kishishita, S.]]		[[Category: Kishishita, S]]
	[[Category: ~~RSGI, RIKEN~~ Structural ~~Genomics/Proteomics Initiative.~~]]		[[Category: Structural genomic]]
	[[Category: Shida, M.]]		[[Category: Shida, M]]
	[[Category: Shirouzu, M.]]		[[Category: Shirouzu, M]]
	[[Category: Takagi, T.]]		[[Category: Takagi, T]]
	[[Category: Yokoyama, S.]]		[[Category: Yokoyama, S]]
	[[Category: Anp]]		[[Category: Anp]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: National project on protein structural and functional analyse]]		[[Category: National project on protein structural and functional analyse]]
	[[Category: Nppsfa]]		[[Category: Nppsfa]]
	~~[[Category: Riken structural genomics/proteomics initiative]]~~
	[[Category: Rsgi]]		[[Category: Rsgi]]
	~~[[Category: Structural genomic]]~~

OCA at 02:05, 29 September 2014

2014-09-29T02:05:34Z

← Older revision		Revision as of 02:05, 29 September 2014
Line 1:		Line 1:
	[[Image:~~2e8a~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP==
			<StructureSection load='2e8a' size='340' side='right' caption='[[2e8a]], [[Resolution\|resolution]] 1.77Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E8A FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2e88\|2e88]]</td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e8a RCSB], [http://www.ebi.ac.uk/pdbsum/2e8a PDBsum], [http://www.topsan.org/Proteins/RSGI/2e8a TOPSAN]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/2e8a_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The 70 kDa heat-shock proteins (Hsp70s) are highly conserved chaperones that are involved in several cellular processes, such as protein folding, disaggregation and translocation. In this study, the crystal structures of the human Hsp70 nucleotide-binding domain (NBD) fragment were determined in the nucleotide-free state and in complex with adenosine 5'-(beta,gamma-imido)triphosphate (AMPPNP). The structure of the nucleotide-free NBD fragment is similar to that of the AMPPNP-bound NBD fragment and is designated as the ;closed form'. In the nucleotide-free NBD fragment the closed form is intrinsically supported through interactions between Tyr15, Lys56 and Glu268 which connect subdomains IA, IB and IIB at the centre of the protein. Interaction with the substrate-binding domain (SBD) of Hsp70 or the BAG domain of BAG1 impairs this subdomain connection and triggers the rotation of subdomain IIA around a hydrophobic helix from subdomain IA. The subdomain rotation is limited by Asp199 and Asp206 from subdomain IIA and clearly defines the open form of the NBD. The open form is further stabilized by a new interaction between Gly230 from subdomain IIB and Ser340 from subdomain IIA. The structure of the NBD in the nucleotide-free state is determined by switching of the inter-subdomain interactions.

	~~{{STRUCTURE_2e8a\| PDB=2e8a \| SCENE= }}~~		Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state.,Shida M, Arakawa A, Ishii R, Kishishita S, Takagi T, Kukimoto-Niino M, Sugano S, Tanaka A, Shirouzu M, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2010 Mar;66(Pt 3):223-32. Epub 2010, Feb 12. PMID:20179333<ref>PMID:20179333</ref>

	~~===Crystal structure~~ of the ~~human Hsp70 ATPase domain in complex with AMP-PNP===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_20179333}}~~

	~~==About this Structure==~~
	~~[[2e8a]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http://oca.weizmann.ac.il~~/~~oca-bin/ocashort?id=2E8A OCA].~~

	==See Also==		==See Also==
	*[[Heat Shock Proteins\|Heat Shock Proteins]]		*[[Heat Shock Proteins\|Heat Shock Proteins]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:020179333<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ishii, R.]]		[[Category: Ishii, R.]]

OCA at 18:09, 20 October 2012

2012-10-20T18:09:24Z

← Older revision		Revision as of 18:09, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2e8a]] is a 1 chain structure ~~of [[Heat Shock Proteins]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA].		[[2e8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8A OCA].

	==See Also==		==See Also==

OCA at 03:11, 27 July 2012

2012-07-27T03:11:44Z

← Older revision		Revision as of 03:11, 27 July 2012
Line 1:		Line 1:
	[[Image:2e8a.png\|left\|200px]]		[[Image:2e8a.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2e8a", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2e8a\| PDB=2e8a \| SCENE= }}		{{STRUCTURE_2e8a\| PDB=2e8a \| SCENE= }}

	===Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP===		===Crystal structure of the human Hsp70 ATPase domain in complex with AMP-PNP===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_20179333}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 20179333 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_20179333}}		{{ABSTRACT_PUBMED_20179333}}

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	==See Also==		==See Also==
	*[[Heat Shock Proteins]]		*[[Heat Shock Proteins\|Heat Shock Proteins]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20179333~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020179333</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ishii, R.]]		[[Category: Ishii, R.]]

OCA: Protected "2e8a" [edit=sysop:move=sysop]

2010-12-26T08:06:06Z

Protected "2e8a" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:06, 26 December 2010
(No difference)