5k9v - Revision history

OCA at 09:56, 27 September 2023

2023-09-27T09:56:39Z

←Older revision		Revision as of 09:56, 27 September 2023
Line 3:		Line 3:
	<StructureSection load='5k9v' size='340' side='right'caption='[[5k9v]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5k9v' size='340' side='right'caption='[[5k9v]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k9v]] 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=5K9V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5K9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k9v]] 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=5K9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9V FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.898Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k9w\|5k9w]]~~, [[~~5ka9~~\|~~5ka9]], [[5ka4\|5ka4]], [[5ka7\|5ka7]], [[5ka8\|5ka8]], [[5ka0\|5ka0]], [[5ka1\|5ka1]], [[5ka2\|5ka2]], [[5ka3\|5ka3]], [[5kaa\|5kaa]], [[5kab\|5kab]], [[5kac\|5kac]], [[5kad\|5kad~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PTPN1, PTP1B ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5k9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9v OCA], [https://pdbe.org/5k9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9v RCSB], [https://www.ebi.ac.uk/pdbsum/5k9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9v ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[http~~:~~//en.wikipedia.org/wiki/Protein~~-~~tyrosine~~-~~phosphatase Protein~~-~~tyrosine~~-~~phosphatase], with EC number [http://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.~~1.3~~.48 3.1.3.48]~~ </~~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=5k9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9v OCA], [~~http~~://pdbe.org/5k9v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5k9v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5k9v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9v ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN]] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>	+	[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:

	==See Also==		==See Also==
-	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]	+	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protein-tyrosine-phosphatase]]~~	+	[[Category: Choy MS]]
-	[[Category: Choy~~, M S~~]]	+	[[Category: Page R]]
-	[[Category: Page, R]]	+	[[Category: Peti W]]
-	[[Category: Peti, W]]	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Protein tyrosine phosphatase~~]]	+

OCA at 12:09, 25 December 2019

2019-12-25T12:09:14Z

←Older revision		Revision as of 12:09, 25 December 2019
Line 1:		Line 1:

	==Protein Tyrosine Phosphatase 1B (1-301), open state==		==Protein Tyrosine Phosphatase 1B (1-301), open state==
-	<StructureSection load='5k9v' size='340' side='right' caption='[[5k9v]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5k9v' size='340' side='right'caption='[[5k9v]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k9v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k9v]] 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=5K9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k9w\|5k9w]], [[5ka9\|5ka9]], [[5ka4\|5ka4]], [[5ka7\|5ka7]], [[5ka8\|5ka8]], [[5ka0\|5ka0]], [[5ka1\|5ka1]], [[5ka2\|5ka2]], [[5ka3\|5ka3]], [[5kaa\|5kaa]], [[5kab\|5kab]], [[5kac\|5kac]], [[5kad\|5kad]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k9w\|5k9w]], [[5ka9\|5ka9]], [[5ka4\|5ka4]], [[5ka7\|5ka7]], [[5ka8\|5ka8]], [[5ka0\|5ka0]], [[5ka1\|5ka1]], [[5ka2\|5ka2]], [[5ka3\|5ka3]], [[5kaa\|5kaa]], [[5kab\|5kab]], [[5kac\|5kac]], [[5kad\|5kad]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTPN1, PTP1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=5k9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9v OCA], [http://pdbe.org/5k9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9v RCSB], [http://www.ebi.ac.uk/pdbsum/5k9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9v 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=5k9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9v OCA], [http://pdbe.org/5k9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9v RCSB], [http://www.ebi.ac.uk/pdbsum/5k9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9v ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5k9v" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5k9v" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Choy, M S]]		[[Category: Choy, M S]]

OCA at 09:35, 11 March 2017

2017-03-11T09:35:53Z

←Older revision		Revision as of 09:35, 11 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5k9v is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Protein Tyrosine Phosphatase 1B (1-301), open state==
		+	<StructureSection load='5k9v' size='340' side='right' caption='[[5k9v]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5k9v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9V FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5k9w\|5k9w]], [[5ka9\|5ka9]], [[5ka4\|5ka4]], [[5ka7\|5ka7]], [[5ka8\|5ka8]], [[5ka0\|5ka0]], [[5ka1\|5ka1]], [[5ka2\|5ka2]], [[5ka3\|5ka3]], [[5kaa\|5kaa]], [[5kab\|5kab]], [[5kac\|5kac]], [[5kad\|5kad]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=5k9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9v OCA], [http://pdbe.org/5k9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9v RCSB], [http://www.ebi.ac.uk/pdbsum/5k9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9v ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN]] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein function originates from a cooperation of structural rigidity, dynamics at different timescales, and allostery. However, how these three pillars of protein function are integrated is still only poorly understood. Here we show how these pillars are connected in Protein Tyrosine Phosphatase 1B (PTP1B), a drug target for diabetes and cancer that catalyzes the dephosphorylation of numerous substrates in essential signaling pathways. By combining new experimental and computational data on WT-PTP1B and >/=10 PTP1B variants in multiple states, we discovered a fundamental and evolutionarily conserved CH/pi switch that is critical for positioning the catalytically important WPD loop. Furthermore, our data show that PTP1B uses conformational and dynamic allostery to regulate its activity. This shows that both conformational rigidity and dynamics are essential for controlling protein activity. This connection between rigidity and dynamics at different timescales is likely a hallmark of all enzyme function.

-	~~Authors~~:	+	Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.,Choy MS, Li Y, Machado LE, Kunze MB, Connors CR, Wei X, Lindorff-Larsen K, Page R, Peti W Mol Cell. 2017 Feb 16;65(4):644-658.e5. doi: 10.1016/j.molcel.2017.01.014. PMID:28212750<ref>PMID:28212750</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5k9v" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Protein-tyrosine-phosphatase]]
		+	[[Category: Choy, M S]]
		+	[[Category: Page, R]]
		+	[[Category: Peti, W]]
		+	[[Category: Hydrolase]]
		+	[[Category: Protein tyrosine phosphatase]]

OCA at 21:16, 23 June 2016

2016-06-23T21:16:53Z

←Older revision		Revision as of 21:16, 23 June 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5k9v is ON HOLD	+	The entry 5k9v is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5k9v" [edit=sysop:move=sysop]

2016-06-20T13:36:52Z

Protected "5k9v" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:36, 20 June 2016

OCA: New page: '''Unreleased structure''' The entry 5k9v is ON HOLD Authors: Description: Category: Unreleased Structures

2016-06-20T13:36:51Z

New page: '''Unreleased structure''' The entry 5k9v is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5k9v is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]