3qkq - Revision history

OCA at 11:49, 14 March 2024

OCA — Thu, 14 Mar 2024 11:49:04 GMT

←Older revision		Revision as of 11:49, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3qkq' size='340' side='right'caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3qkq' size='340' side='right'caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2~~-~~AMINO-2-HYDROXYMETHYL-PROPANE-1~~,~~3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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]] 2.2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ptp1b, ptpn1 ([https://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'>[https~~:~~//en.wikipedia.org/wiki/Protein~~-~~tyrosine~~-~~phosphatase Protein~~-~~tyrosine~~-~~phosphatase]~~, ~~with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [https://pdbe.org/3qkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [https://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq 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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [https://pdbe.org/3qkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [https://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The movement of a conserved protein loop (the WPD-loop) is important in catalysis by protein tyrosine phosphatases (PTPs). Using kinetics, isotope effects, and X-ray crystallography, the different effects arising from mutation of the conserved tryptophan in the WPD-loop were compared in two PTPs, the human PTP1B, and the bacterial YopH from Yersinia. Mutation of the conserved tryptophan in the WPD-loop to phenylalanine has a negligible effect on k(cat) in PTP1B and full loop movement is maintained. In contrast, the corresponding mutation in YopH reduces k(cat) by two orders of magnitude and the WPD loop locks in an intermediate position, disabling general acid catalysis. During loop movement the indole moiety of the WPD-loop tryptophan moves in opposite directions in the two enzymes. Comparisons of mammalian and bacterial PTPs reveal differences in the residues forming the hydrophobic pocket surrounding the conserved tryptophan. Thus, although WPD-loop movement is a conserved feature in PTPs, differences exist in the molecular details, and in the tolerance to mutation, in PTP1B compared to YopH. Despite high structural similarity of the active sites in both WPD-loop open and closed conformations, differences are identified in the molecular details associated with loop movement in PTPs from different organisms.	+
-		+
-	The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.,Brandao TA, Johnson SJ, Hengge AC Arch Biochem Biophys. 2012 Sep 1;525(1):53-9. Epub 2012 Jun 12. PMID:22698963<ref>PMID:22698963</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3qkq" style="background-color:#fffaf0;"></div>~~	+
-		+
-	~~==See Also==~~	+
-	*[[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: Brandao TAS]]
-	[[Category: Brandao~~, T A.S~~]]	+	[[Category: Hengge AC]]
-	[[Category: Hengge~~, A C~~]]	+	[[Category: Johnson SJ]]
-	[[Category: Johnson~~, S J]]~~	+
-	~~[[Category: Egfr receptor]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: P-loop]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Protein phosphatase]]~~	+
-	~~[[Category: Vanadate]]~~	+
-	~~[[Category: Wpd-loop~~]]	+

OCA at 06:12, 8 June 2022

OCA — Wed, 08 Jun 2022 06:12:56 GMT

←Older revision		Revision as of 06:12, 8 June 2022
Line 1:		Line 1:

	==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==		==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==
-	<StructureSection load='3qkq' size='340' side='right' caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='3qkq' size='340' side='right'caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([https://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'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [~~http~~://pdbe.org/3qkq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq 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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [https://pdbe.org/3qkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [https://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq 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 23:

	==See Also==		==See Also==
-	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]	+	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Brandao, T A.S]]		[[Category: Brandao, T A.S]]

OCA at 10:49, 5 August 2016

OCA — Fri, 05 Aug 2016 10:49:16 GMT

←Older revision		Revision as of 10:49, 5 August 2016
Line 1:		Line 1:
		+
	==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==		==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==
	<StructureSection load='3qkq' size='340' side='right' caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3qkq' size='340' side='right' caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum]</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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://pdbe.org/3qkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3qkq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Brandao, T A.S]]		[[Category: Brandao, T A.S]]

OCA at 01:43, 25 December 2014

OCA — Thu, 25 Dec 2014 01:43:50 GMT

←Older revision		Revision as of 01:43, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum]</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=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum]</span></td></tr>
-	<table>	+	</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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 28:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
-	[[Category: Brandao, T A.S.]]	+	[[Category: Brandao, T A.S]]
-	[[Category: Hengge, A C.]]	+	[[Category: Hengge, A C]]
-	[[Category: Johnson, S J.]]	+	[[Category: Johnson, S J]]
	[[Category: Egfr receptor]]		[[Category: Egfr receptor]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 06:52, 9 June 2014

OCA — Mon, 09 Jun 2014 06:52:26 GMT

←Older revision		Revision as of 06:52, 9 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3qkq.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate==
		+	<StructureSection load='3qkq' size='340' side='right' caption='[[3qkq]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3qkq]] 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=3QKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QKQ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cm2\|2cm2]], [[3f9b\|3f9b]], [[3qkn\|3qkn]], [[3qko\|3qko]], [[3qkp\|3qkp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ptp1b, ptpn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkq RCSB], [http://www.ebi.ac.uk/pdbsum/3qkq PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The movement of a conserved protein loop (the WPD-loop) is important in catalysis by protein tyrosine phosphatases (PTPs). Using kinetics, isotope effects, and X-ray crystallography, the different effects arising from mutation of the conserved tryptophan in the WPD-loop were compared in two PTPs, the human PTP1B, and the bacterial YopH from Yersinia. Mutation of the conserved tryptophan in the WPD-loop to phenylalanine has a negligible effect on k(cat) in PTP1B and full loop movement is maintained. In contrast, the corresponding mutation in YopH reduces k(cat) by two orders of magnitude and the WPD loop locks in an intermediate position, disabling general acid catalysis. During loop movement the indole moiety of the WPD-loop tryptophan moves in opposite directions in the two enzymes. Comparisons of mammalian and bacterial PTPs reveal differences in the residues forming the hydrophobic pocket surrounding the conserved tryptophan. Thus, although WPD-loop movement is a conserved feature in PTPs, differences exist in the molecular details, and in the tolerance to mutation, in PTP1B compared to YopH. Despite high structural similarity of the active sites in both WPD-loop open and closed conformations, differences are identified in the molecular details associated with loop movement in PTPs from different organisms.

-	~~{{STRUCTURE_3qkq\| PDB=3qkq \| SCENE= }}~~	+	The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.,Brandao TA, Johnson SJ, Hengge AC Arch Biochem Biophys. 2012 Sep 1;525(1):53-9. Epub 2012 Jun 12. PMID:22698963<ref>PMID:22698963</ref>

-	~~===Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_22698963}}~~	+	==See Also==
-		+	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~3qkq~~]] 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=3QKQ OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:022698963<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]

OCA at 05:22, 8 August 2012

OCA — Wed, 08 Aug 2012 05:22:53 GMT

←Older revision		Revision as of 05:22, 8 August 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3qkq.jpg\|left\|200px]]

-	~~The entry~~ 3qkq ~~is ON HOLD~~ ~~until Aug 08 2013~~	+	{{STRUCTURE_3qkq\| PDB=3qkq \| SCENE= }}

-	~~Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.~~	+	===Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate===

-	~~Description~~: Protein ~~Tyrosine Phosphatase 1B~~ -~~W179F mutant bound with vanadate~~	+	{{ABSTRACT_PUBMED_22698963}}
		+
		+	==About this Structure==
		+	[[3qkq]] 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=3QKQ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022698963</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Protein-tyrosine-phosphatase]]
		+	[[Category: Brandao, T A.S.]]
		+	[[Category: Hengge, A C.]]
		+	[[Category: Johnson, S J.]]
		+	[[Category: Egfr receptor]]
		+	[[Category: Hydrolase]]
		+	[[Category: P-loop]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Protein phosphatase]]
		+	[[Category: Vanadate]]
		+	[[Category: Wpd-loop]]

OCA at 08:32, 9 May 2012

OCA — Wed, 09 May 2012 08:32:40 GMT

←Older revision		Revision as of 08:32, 9 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qkq is ON HOLD until ~~May 09~~ 2013	+	The entry 3qkq is ON HOLD until Aug 08 2013

	Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.		Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.

	Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate		Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate

OCA at 06:24, 11 April 2012

OCA — Wed, 11 Apr 2012 06:24:58 GMT

←Older revision		Revision as of 06:24, 11 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qkq is ON HOLD until May 01 2013	+	The entry 3qkq is ON HOLD until May 09 2013

	Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.		Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.

	Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate		Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate

OCA at 06:39, 1 February 2012

OCA — Wed, 01 Feb 2012 06:39:59 GMT

←Older revision		Revision as of 06:39, 1 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qkq is ON HOLD until ~~Feb~~ 01 2013	+	The entry 3qkq is ON HOLD until May 01 2013

	Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.		Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.

	Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate		Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate

OCA at 06:33, 28 December 2011

OCA — Wed, 28 Dec 2011 06:33:31 GMT

←Older revision		Revision as of 06:33, 28 December 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qkq is ON HOLD until ~~Paper Publication~~	+	The entry 3qkq is ON HOLD until Feb 01 2013

	Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.		Authors: Brandao, T.A.S., Johnson, S.J., Hengge, A.C.

	Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate		Description: Protein Tyrosine Phosphatase 1B -W179F mutant bound with vanadate