5j28 - Revision history

OCA at 10:42, 6 September 2023

2023-09-06T10:42:51Z

←Older revision		Revision as of 10:42, 6 September 2023
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	<StructureSection load='5j28' size='340' side='right'caption='[[5j28]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5j28' size='340' side='right'caption='[[5j28]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j28]] is a 4 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=5J28 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5J28 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j28]] is a 4 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=5J28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J28 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5inb\|5inb]]~~, [[~~5ioh~~\|~~5ioh~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PPP1CC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN]), MKI67 ([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=5j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j28 OCA], [https://pdbe.org/5j28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j28 RCSB], [https://www.ebi.ac.uk/pdbsum/5j28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j28 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=5j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j28 OCA], [~~http~~://pdbe.org/5j28 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5j28 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5j28 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5j28 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_HUMAN]] 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</ref> ~~[[http://www.uniprot.org/uniprot/KI67_HUMAN KI67_HUMAN]] Thought to be required for maintaining cell proliferation.~~	+	[https://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_HUMAN] 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Phosphoprotein phosphatase]]~~	+	[[Category: Kumar GS]]
-	[[Category: Kumar~~, G S~~]]	+	[[Category: Page R]]
-	[[Category: Page, R]]	+	[[Category: Peti W]]
-	[[Category: Peti, W]]	+
-	~~[[Category: Hydrolase-protein binding complex]]~~	+
-	~~[[Category: Ki-67]]~~	+
-	~~[[Category: Phosphatase]]~~	+
-	~~[[Category: Pp1 gamma]]~~	+
-	~~[[Category: Repoman~~]]	+

OCA at 08:53, 18 December 2019

2019-12-18T08:53:30Z

←Older revision		Revision as of 08:53, 18 December 2019
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	==Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex==		==Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex==
-	<StructureSection load='5j28' size='340' side='right' caption='[[5j28]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5j28' size='340' side='right'caption='[[5j28]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j28]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J28 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j28]] is a 4 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=5J28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J28 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5inb\|5inb]], [[5ioh\|5ioh]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5inb\|5inb]], [[5ioh\|5ioh]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPP1CC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MKI67 ([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/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=5j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j28 OCA], [http://pdbe.org/5j28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j28 RCSB], [http://www.ebi.ac.uk/pdbsum/5j28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j28 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=5j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j28 OCA], [http://pdbe.org/5j28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j28 RCSB], [http://www.ebi.ac.uk/pdbsum/5j28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j28 ProSAT]</span></td></tr>
Line 22:		Line 23:

	==See Also==		==See Also==
-	*[[~~Serine/threonine protein~~ phosphatase\|~~Serine/threonine protein~~ phosphatase]]	+	*[[Protein phosphatase 3D structures\|Protein phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
	[[Category: Kumar, G S]]		[[Category: Kumar, G S]]

OCA at 12:53, 6 November 2017

2017-11-06T12:53:00Z

←Older revision		Revision as of 12:53, 6 November 2017
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[~~Protein~~ phosphatase\|~~Protein~~ phosphatase]]	+	*[[Serine/threonine protein phosphatase\|Serine/threonine protein phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:33, 27 September 2017

2017-09-27T09:33:17Z

←Older revision		Revision as of 09:33, 27 September 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5j28" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5j28" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Protein phosphatase\|Protein phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:15, 19 October 2016

2016-10-19T09:15:33Z

←Older revision		Revision as of 09:15, 19 October 2016
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_HUMAN]] 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</ref> [[http://www.uniprot.org/uniprot/KI67_HUMAN KI67_HUMAN]] Thought to be required for maintaining cell proliferation.		[[http://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_HUMAN]] 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</ref> [[http://www.uniprot.org/uniprot/KI67_HUMAN KI67_HUMAN]] Thought to be required for maintaining cell proliferation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ki-67 and RepoMan have key roles during mitotic exit. Previously, we showed that Ki-67 organizes the mitotic chromosome periphery and recruits protein phosphatase 1 (PP1) to chromatin at anaphase onset, in a similar manner as RepoMan (Booth et al., 2014). Here we show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis. Unexpectedly, our data also reveal that Ki-67 and RepoMan bind PP1 using an identical, yet novel mechanism, interacting with a PP1 pocket that is engaged only by these two PP1 regulators. These findings not only show how two distinct mitotic exit phosphatases are recruited to their substrates, but also provide immediate opportunities for the design of novel cancer therapeutics that selectively target the Ki-67:PP1 and RepoMan:PP1 holoenzymes.
		+
		+	The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism.,Kumar GS, Gokhan E, De Munter S, Bollen M, Vagnarelli P, Peti W, Page R Elife. 2016 Aug 30;5. pii: e16539. doi: 10.7554/eLife.16539. PMID:27572260<ref>PMID:27572260</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5j28" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:29, 5 October 2016

2016-10-05T21:29:50Z

←Older revision		Revision as of 21:29, 5 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5j28 is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex==
-		+	<StructureSection load='5j28' size='340' side='right' caption='[[5j28]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5j28]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J28 FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5inb\|5inb]], [[5ioh\|5ioh]]</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=5j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j28 OCA], [http://pdbe.org/5j28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j28 RCSB], [http://www.ebi.ac.uk/pdbsum/5j28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j28 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_HUMAN]] 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</ref> [[http://www.uniprot.org/uniprot/KI67_HUMAN KI67_HUMAN]] Thought to be required for maintaining cell proliferation.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Phosphoprotein phosphatase]]
		+	[[Category: Kumar, G S]]
		+	[[Category: Page, R]]
		+	[[Category: Peti, W]]
		+	[[Category: Hydrolase-protein binding complex]]
		+	[[Category: Ki-67]]
		+	[[Category: Phosphatase]]
		+	[[Category: Pp1 gamma]]
		+	[[Category: Repoman]]

OCA at 11:45, 27 July 2016

2016-07-27T11:45:57Z

←Older revision		Revision as of 11:45, 27 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5j28 is ON HOLD	+	The entry 5j28 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 14:59, 15 May 2016

2016-05-15T14:59:08Z

←Older revision		Revision as of 14:59, 15 May 2016
Line 3:		Line 3:
	The entry 5j28 is ON HOLD		The entry 5j28 is ON HOLD

-	Authors: ~~Kumar, G.S., Peti, W., Page, R.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Page, R]]
-	[[Category: Kumar, G.S]]
-	[[Category: Peti, W]]

OCA: Protected "5j28" [edit=sysop:move=sysop]

2016-05-11T01:20:46Z

Protected "5j28" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:20, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5j28 is ON HOLD Authors: Kumar, G.S., Peti, W., Page, R. Description: Category: Unreleased Structures Category: Page, R [[Category: Kumar,...

2016-05-11T01:20:45Z

New page: '''Unreleased structure''' The entry 5j28 is ON HOLD Authors: Kumar, G.S., Peti, W., Page, R. Description: Category: Unreleased Structures Category: Page, R [[Category: Kumar,...

New page

'''Unreleased structure'''

The entry 5j28 is ON HOLD

Authors: Kumar, G.S., Peti, W., Page, R.

Description:
[[Category: Unreleased Structures]]
[[Category: Page, R]]
[[Category: Kumar, G.S]]
[[Category: Peti, W]]