4v0w - Revision history

OCA at 07:20, 1 May 2024

2024-05-01T07:20:06Z

←Older revision		Revision as of 07:20, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V0W FirstGlance]. <br>		<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V0W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.55Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [https://pdbe.org/4v0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [https://www.ebi.ac.uk/pdbsum/4v0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v0w 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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [https://pdbe.org/4v0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [https://www.ebi.ac.uk/pdbsum/4v0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PP1G_MOUSE PP1G_MOUSE] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.<ref>PMID:21712997</ref> <ref>PMID:21930935</ref>		[https://www.uniprot.org/uniprot/PP1G_MOUSE PP1G_MOUSE] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.<ref>PMID:21712997</ref> <ref>PMID:21930935</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Dephosphorylation of eukaryotic translation initiation factor 2a (eIF2a) restores protein synthesis at the waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A/GADD34 or PPP1R15B/CReP. Surprisingly, PPP1R15-PP1 binary complexes reconstituted in vitro lacked substrate selectivity. However, selectivity was restored by crude cell lysate or purified G-actin, which joined PPP1R15-PP1 to form a stable ternary complex. In crystal structures of the non-selective PPP1R15B-PP1G complex, the functional core of PPP1R15 made multiple surface contacts with PP1G, but at a distance from the active site, whereas in the substrate-selective ternary complex, actin contributes to one face of a platform encompassing the active site. Computational docking of the N-terminal lobe of eIF2a at this platform placed phosphorylated serine 51 near the active site. Mutagenesis of predicted surface-contacting residues enfeebled dephosphorylation, suggesting that avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.
-
-	G-actin provides substrate-specificity to eukaryotic initiation factor 2alpha holophosphatases.,Chen R, Rato C, Yan Y, Crespillo-Casado A, Clarke HJ, Harding HP, Marciniak SJ, Read RJ, Ron D Elife. 2015 Mar 16;4. doi: 10.7554/eLife.04871. PMID:25774600<ref>PMID:25774600</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4v0w" style="background-color:#fffaf0;"></div>

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

OCA at 07:56, 29 March 2023

2023-03-29T07:56:38Z

←Older revision		Revision as of 07:56, 29 March 2023
Line 1:		Line 1:

	==The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)==		==The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)==
-	<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='4v0w' size='340' side='right'caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4V0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V0W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [https://pdbe.org/4v0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [https://www.ebi.ac.uk/pdbsum/4v0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v0w 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/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [~~http~~://pdbe.org/4v0w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4v0w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4v0w ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PP1G_MOUSE PP1G_MOUSE]] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.<ref>PMID:21712997</ref> <ref>PMID:21930935</ref> ~~[[http://www.uniprot.org/uniprot/PR15B_HUMAN PR15B_HUMAN]] Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.~~	+	[https://www.uniprot.org/uniprot/PP1G_MOUSE PP1G_MOUSE] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.<ref>PMID:21712997</ref> <ref>PMID:21930935</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4v0w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4v0w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Protein phosphatase 3D structures\|Protein phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Phosphoprotein phosphatase~~]]	+	[[Category: Mus musculus]]
-	[[Category: Casado~~, A C~~]]	+	[[Category: Casado AC]]
-	[[Category: Chen, R]]	+	[[Category: Chen R]]
-	[[Category: Read~~, R J~~]]	+	[[Category: Read RJ]]
-	[[Category: Ron, D]]	+	[[Category: Ron D]]
-	[[Category: Yan, Y]]	+	[[Category: Yan Y]]
-	~~[[Category: Hydrolase-hydrolase regulator complex~~]]	+

OCA at 15:47, 27 February 2019

2019-02-27T15:47:04Z

←Older revision		Revision as of 15:47, 27 February 2019
Line 3:		Line 3:
	<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V0W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</td></tr>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4v0w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4v0w" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Serine/threonine protein phosphatase\|Serine/threonine protein phosphatase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
	[[Category: Casado, A C]]		[[Category: Casado, A C]]

OCA at 01:18, 19 January 2017

2017-01-19T01:18:45Z

←Older revision		Revision as of 01:18, 19 January 2017
Line 1:		Line 1:
		+
	==The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)==		==The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)==
	<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [http://www.ebi.ac.uk/pdbsum/4v0w 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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [http://pdbe.org/4v0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [http://www.ebi.ac.uk/pdbsum/4v0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4v0w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein phosphatase\|Serine/threonine protein phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:56, 26 March 2015

2015-03-26T13:56:44Z

←Older revision		Revision as of 13:56, 26 March 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)==
		+	<StructureSection load='4v0w' size='340' side='right' caption='[[4v0w]], [[Resolution\|resolution]] 1.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4v0w]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V0W FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4v0u\|4v0u]], [[4v0v\|4v0v]], [[4v0x\|4v0x]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=4v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v0w RCSB], [http://www.ebi.ac.uk/pdbsum/4v0w PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PP1G_MOUSE PP1G_MOUSE]] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.<ref>PMID:21712997</ref> <ref>PMID:21930935</ref> [[http://www.uniprot.org/uniprot/PR15B_HUMAN PR15B_HUMAN]] Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dephosphorylation of eukaryotic translation initiation factor 2a (eIF2a) restores protein synthesis at the waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A/GADD34 or PPP1R15B/CReP. Surprisingly, PPP1R15-PP1 binary complexes reconstituted in vitro lacked substrate selectivity. However, selectivity was restored by crude cell lysate or purified G-actin, which joined PPP1R15-PP1 to form a stable ternary complex. In crystal structures of the non-selective PPP1R15B-PP1G complex, the functional core of PPP1R15 made multiple surface contacts with PP1G, but at a distance from the active site, whereas in the substrate-selective ternary complex, actin contributes to one face of a platform encompassing the active site. Computational docking of the N-terminal lobe of eIF2a at this platform placed phosphorylated serine 51 near the active site. Mutagenesis of predicted surface-contacting residues enfeebled dephosphorylation, suggesting that avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.

-	~~The entry 4v0w is ON HOLD until Paper Publication~~	+	G-actin provides substrate-specificity to eukaryotic initiation factor 2alpha holophosphatases.,Chen R, Rato C, Yan Y, Crespillo-Casado A, Clarke HJ, Harding HP, Marciniak SJ, Read RJ, Ron D Elife. 2015 Mar 16;4. doi: 10.7554/eLife.04871. PMID:25774600<ref>PMID:25774600</ref>

-	~~Authors: Chen~~, R.~~, Yan, Y~~.~~, Casado, A.C., Ron, D., Read, R.J~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Phosphoprotein phosphatase]]
		+	[[Category: Casado, A C]]
	[[Category: Chen, R]]		[[Category: Chen, R]]
-	[[Category: ~~Casado~~, ~~A.C~~]]	+	[[Category: Read, R J]]
	[[Category: Ron, D]]		[[Category: Ron, D]]
-	[[Category: Read, R.J]]
	[[Category: Yan, Y]]		[[Category: Yan, Y]]
		+	[[Category: Hydrolase-hydrolase regulator complex]]

OCA at 18:57, 24 December 2014

2014-12-24T18:57:46Z

←Older revision		Revision as of 18:57, 24 December 2014
Line 6:		Line 6:

	Description: The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)		Description: The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)
		+	[[Category: Unreleased Structures]]
		+	[[Category: Chen, R]]
		+	[[Category: Casado, A.C]]
		+	[[Category: Ron, D]]
		+	[[Category: Read, R.J]]
		+	[[Category: Yan, Y]]

OCA at 09:43, 24 December 2014

2014-12-24T09:43:03Z

←Older revision		Revision as of 09:43, 24 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4v0w is ON HOLD	+	The entry 4v0w is ON HOLD until Paper Publication

	Authors: Chen, R., Yan, Y., Casado, A.C., Ron, D., Read, R.J.		Authors: Chen, R., Yan, Y., Casado, A.C., Ron, D., Read, R.J.

	Description: The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)		Description: The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)

OCA: Protected "4v0w" [edit=sysop:move=sysop]

2014-09-24T08:59:41Z

Protected "4v0w" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:59, 24 September 2014

OCA: New page: '''Unreleased structure''' The entry 4v0w is ON HOLD Authors: Chen, R., Yan, Y., Casado, A.C., Ron, D., Read, R.J. Description: The crystal structure of mouse PP1G in complex with trun...

2014-09-24T08:59:39Z

New page: '''Unreleased structure''' The entry 4v0w is ON HOLD Authors: Chen, R., Yan, Y., Casado, A.C., Ron, D., Read, R.J. Description: The crystal structure of mouse PP1G in complex with trun...

New page

'''Unreleased structure'''

The entry 4v0w is ON HOLD

Authors: Chen, R., Yan, Y., Casado, A.C., Ron, D., Read, R.J.

Description: The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)