7f50 - Revision history

OCA at 17:09, 29 November 2023

2023-11-29T17:09:37Z

←Older revision		Revision as of 17:09, 29 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7f50]] 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=7F50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F50 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7f50]] 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=7F50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F50 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=CL:CHLORIDE+ION'>CL</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]] 1.703Å</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=CL:CHLORIDE+ION'>CL</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=7f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f50 OCA], [https://pdbe.org/7f50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f50 RCSB], [https://www.ebi.ac.uk/pdbsum/7f50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f50 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=7f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f50 OCA], [https://pdbe.org/7f50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f50 RCSB], [https://www.ebi.ac.uk/pdbsum/7f50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f50 ProSAT]</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/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>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:01, 14 September 2022

2022-09-14T07:01:27Z

←Older revision		Revision as of 07:01, 14 September 2022
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	==X-ray crystal structure of Y149A mutated Hsp72-NBD in complex with AMPPnP==		==X-ray crystal structure of Y149A mutated Hsp72-NBD in complex with AMPPnP==
-	<StructureSection load='7f50' size='340' side='right'caption='[[7f50]]' scene=''>	+	<StructureSection load='7f50' size='340' side='right'caption='[[7f50]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F50 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7f50]] 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=7F50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F50 FirstGlance]. <br>
-	</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=7f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f50 OCA], [https://pdbe.org/7f50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f50 RCSB], [https://www.ebi.ac.uk/pdbsum/7f50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f50 ProSAT]</span></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=CL:CHLORIDE+ION'>CL</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=7f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f50 OCA], [https://pdbe.org/7f50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f50 RCSB], [https://www.ebi.ac.uk/pdbsum/7f50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f50 ProSAT]</span></td></tr>
	</table>		</table>
		+	== 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>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Yokoyama, T,~~ Fujii, S~~, Nabeshima, Y,~~ Mizuguchi, M]]	+	[[Category: Fujii S]]
		+	[[Category: Mizuguchi M]]
		+	[[Category: Nabeshima Y]]
		+	[[Category: Yokoyama T]]

OCA at 07:25, 29 June 2022

2022-06-29T07:25:31Z

←Older revision		Revision as of 07:25, 29 June 2022
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-	'''Unreleased structure'''

-	~~The entry 7f50 is ON HOLD until Paper Publication~~	+	==X-ray crystal structure of Y149A mutated Hsp72-NBD in complex with AMPPnP==
-		+	<StructureSection load='7f50' size='340' side='right'caption='[[7f50]]' scene=''>
-	~~Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F50 FirstGlance]. <br>
-	~~Description:~~ X-ray crystal structure of Y149A mutated Hsp72-NBD in complex with AMPPnP	+	</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=7f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f50 OCA], [https://pdbe.org/7f50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f50 RCSB], [https://www.ebi.ac.uk/pdbsum/7f50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f50 ProSAT]</span></td></tr>
-	[[~~Category: Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Nabeshima, Y]~~]	+	__TOC__
-	[[~~Category~~: ~~Fujii~~, S]]	+	</StructureSection>
-	[[Category: ~~Yokoyama, T~~]]	+	[[Category: Large Structures]]
-	[[Category: Mizuguchi, M]]	+	[[Category: Yokoyama, T, Fujii, S, Nabeshima, Y, Mizuguchi, M]]

OCA at 06:19, 22 June 2022

2022-06-22T06:19:49Z

←Older revision		Revision as of 06:19, 22 June 2022
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Nabeshima, Y]]		[[Category: Nabeshima, Y]]
-	[[Category: Yokoyama, T]]
	[[Category: Fujii, S]]		[[Category: Fujii, S]]
		+	[[Category: Yokoyama, T]]
	[[Category: Mizuguchi, M]]		[[Category: Mizuguchi, M]]

OCA at 11:57, 17 November 2021

2021-11-17T11:57:19Z

←Older revision		Revision as of 11:57, 17 November 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7f50 is ON HOLD	+	The entry 7f50 is ON HOLD until Paper Publication

	Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M.		Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M.

OCA: Protected "7f50" [edit=sysop:move=sysop]

2021-07-02T02:23:48Z

Protected "7f50" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:23, 2 July 2021

OCA: New page: '''Unreleased structure''' The entry 7f50 is ON HOLD Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M. Description: X-ray crystal structure of Y149A mutated Hsp72-NBD in c...

2021-07-02T02:23:47Z

New page: '''Unreleased structure''' The entry 7f50 is ON HOLD Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M. Description: X-ray crystal structure of Y149A mutated Hsp72-NBD in c...

New page

'''Unreleased structure'''

The entry 7f50 is ON HOLD

Authors: Yokoyama, T., Fujii, S., Nabeshima, Y., Mizuguchi, M.

Description: X-ray crystal structure of Y149A mutated Hsp72-NBD in complex with AMPPnP
[[Category: Unreleased Structures]]
[[Category: Nabeshima, Y]]
[[Category: Yokoyama, T]]
[[Category: Fujii, S]]
[[Category: Mizuguchi, M]]