3n5u - Revision history

OCA at 10:28, 21 February 2024

2024-02-21T10:28:02Z

←Older revision		Revision as of 10:28, 21 February 2024
Line 1:		Line 1:

	==Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1==		==Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1==
-	<StructureSection load='3n5u' size='340' side='right' caption='[[3n5u]], [[Resolution\|resolution]] 3.20Å' scene=''>	+	<StructureSection load='3n5u' size='340' side='right'caption='[[3n5u]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3n5u]] is a 3 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=3N5U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3N5U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3n5u]] is a 3 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=3N5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N5U 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=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]] 3.2Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PPP1A, PPP1CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</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=MN:MANGANESE+(II)+ION'>MN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5u OCA], [https://pdbe.org/3n5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n5u RCSB], [https://www.ebi.ac.uk/pdbsum/3n5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5u 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=3n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5u OCA], [~~http~~://pdbe.org/3n5u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3n5u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3n5u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5u ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Defects in RB1 are the cause of childhood cancer retinoblastoma (RB) [MIM:[http://omim.org/entry/180200 180200]]. RB is a congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated.<ref>PMID:2594029</ref> <ref>PMID:1352883</ref> <ref>PMID:8346255</ref> <ref>PMID:7704558</ref> <ref>PMID:7927327</ref> <ref>PMID:8605116</ref> <ref>PMID:7795591</ref> <ref>PMID:8776589</ref> <ref>PMID:9311732</ref> <ref>PMID:9140452</ref> <ref>PMID:10671068</ref> <ref>PMID:9973307</ref> <ref>PMID:11524739</ref> Defects in RB1 are a cause of susceptibility to bladder cancer (BLC) [MIM:[http://omim.org/entry/109800 109800]]. A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in RB1 are a cause of osteogenic sarcoma (OSRC) [MIM:[http://omim.org/entry/259500 259500]].
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref> [[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.<ref>PMID:15084261</ref>	+	[https://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n5u_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n5u_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 23:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3n5u ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3n5u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The phosphorylation state and corresponding activity of the retinoblastoma tumor suppressor protein (Rb) are modulated by a balance of kinase and phosphatase activities. Here we characterize the association of Rb with the catalytic subunit of protein phosphatase 1 (PP1c). A crystal structure identifies an enzyme docking site in the Rb C-terminal domain that is required for efficient PP1c activity toward Rb. The phosphatase docking site overlaps with the known docking site for cyclin-dependent kinase (Cdk), and PP1 competition with Cdk-cyclins for Rb binding is sufficient to retain Rb activity and block cell-cycle advancement. These results provide the first detailed molecular insights into Rb activation and establish a novel mechanism for Rb regulation in which kinase and phosphatase compete for substrate docking.
-
-	An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein.,Hirschi A, Cecchini M, Steinhardt RC, Schamber MR, Dick FA, Rubin SM Nat Struct Mol Biol. 2010 Sep;17(9):1051-7. Epub 2010 Aug 8. PMID:20694007<ref>PMID:20694007</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3n5u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Protein phosphatase\|Protein phosphatase]]	+	*[[Protein phosphatase 3D structures\|Protein phosphatase 3D structures]]
-	*[[Serine/threonine protein phosphatase\|Serine/threonine protein phosphatase]]	+
-	*[[User:Iris To/Retinoblastoma Protein Regulation\|User:Iris To/Retinoblastoma Protein Regulation]]	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Phosphoprotein phosphatase~~]]	+	[[Category: Large Structures]]
-	[[Category: Cecchini, M]]	+	[[Category: Cecchini M]]
-	[[Category: Dick~~, F A~~]]	+	[[Category: Dick FA]]
-	[[Category: Hirschi~~, A M~~]]	+	[[Category: Hirschi AM]]
-	[[Category: Rubin~~, S M~~]]	+	[[Category: Rubin SM]]
-	[[Category: Steinhardt~~, R C]]~~	+	[[Category: Steinhardt RC]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Phosphatase]]~~	+
-	~~[[Category: Pp1]]~~	+
-	~~[[Category: Prb]]~~	+
-	~~[[Category: Protein phosphatase-1]]~~	+
-	~~[[Category: Rb]]~~	+
-	~~[[Category: Retinoblastoma]]~~	+
-	~~[[Category: Transcription regulation~~]]	+

OCA at 08:11, 5 August 2016

2016-08-05T08:11:10Z

←Older revision		Revision as of 08:11, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1==		==Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1==
	<StructureSection load='3n5u' size='340' side='right' caption='[[3n5u]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='3n5u' size='340' side='right' caption='[[3n5u]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3n5u]] is a 3 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=3N5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3n5u]] is a 3 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=3N5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5U 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=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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPP1A, PPP1CA ([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">PPP1A, PPP1CA ([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=3n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5u RCSB], [http://www.ebi.ac.uk/pdbsum/3n5u 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=3n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5u OCA], [http://pdbe.org/3n5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n5u RCSB], [http://www.ebi.ac.uk/pdbsum/3n5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5u ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3n5u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	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 3n5u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 41:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
	[[Category: Cecchini, M]]		[[Category: Cecchini, M]]

OCA at 14:55, 18 December 2014

2014-12-18T14:55:29Z

←Older revision		Revision as of 14:55, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3n5u\| PDB=3n5u \| SCENE= }}~~	+	==Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1==
-	===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===	+	<StructureSection load='3n5u' size='340' side='right' caption='[[3n5u]], [[Resolution\|resolution]] 3.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20694007}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3n5u]] is a 3 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=3N5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5U 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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPP1A, PPP1CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5u RCSB], [http://www.ebi.ac.uk/pdbsum/3n5u PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Defects in RB1 are the cause of childhood cancer retinoblastoma (RB) [MIM:[http://omim.org/entry/180200 180200]]. RB is a congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated.<ref>PMID:2594029</ref> <ref>PMID:1352883</ref> <ref>PMID:8346255</ref> <ref>PMID:7704558</ref> <ref>PMID:7927327</ref> <ref>PMID:8605116</ref> <ref>PMID:7795591</ref> <ref>PMID:8776589</ref> <ref>PMID:9311732</ref> <ref>PMID:9140452</ref> <ref>PMID:10671068</ref> <ref>PMID:9973307</ref> <ref>PMID:11524739</ref> Defects in RB1 are a cause of susceptibility to bladder cancer (BLC) [MIM:[http://omim.org/entry/109800 109800]]. A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in RB1 are a cause of osteogenic sarcoma (OSRC) [MIM:[http://omim.org/entry/259500 259500]].
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref> [[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.<ref>PMID:15084261</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n5u_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The phosphorylation state and corresponding activity of the retinoblastoma tumor suppressor protein (Rb) are modulated by a balance of kinase and phosphatase activities. Here we characterize the association of Rb with the catalytic subunit of protein phosphatase 1 (PP1c). A crystal structure identifies an enzyme docking site in the Rb C-terminal domain that is required for efficient PP1c activity toward Rb. The phosphatase docking site overlaps with the known docking site for cyclin-dependent kinase (Cdk), and PP1 competition with Cdk-cyclins for Rb binding is sufficient to retain Rb activity and block cell-cycle advancement. These results provide the first detailed molecular insights into Rb activation and establish a novel mechanism for Rb regulation in which kinase and phosphatase compete for substrate docking.

-	~~==Disease==~~	+	An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein.,Hirschi A, Cecchini M, Steinhardt RC, Schamber MR, Dick FA, Rubin SM Nat Struct Mol Biol. 2010 Sep;17(9):1051-7. Epub 2010 Aug 8. PMID:20694007<ref>PMID:20694007</ref>
-	~~[[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Defects in RB1 are~~ the ~~cause of childhood cancer~~ retinoblastoma ~~(RB) [MIM:[http://omim~~.org/entry/180200 180200]]. RB is a congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, ~~about 20% are transmitted as an autosomal dominant trait with incomplete penetrance~~. ~~The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil~~ (~~'cat eye'~~) ~~is investigated~~.~~<ref>~~PMID:~~2594029</ref>~~<ref>PMID:~~1352883~~</ref><ref>PMID:8346255</ref><ref>PMID:7704558</ref><ref>PMID:7927327</ref><ref>PMID:8605116</ref><ref>PMID:7795591</ref><ref>PMID:8776589</ref><ref>PMID:9311732</ref><ref>PMID:9140452</ref><ref>PMID:10671068</ref><ref>PMID:9973307</ref><ref>PMID:11524739</ref> Defects in RB1 are a cause of susceptibility to bladder cancer (BLC) [MIM:[http://omim.org/entry/109800 109800]]. A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in RB1 are a cause of osteogenic sarcoma (OSRC) [MIM:[http://omim.org/entry/259500 259500]].	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~//www.uniprot.org/uniprot/PP1A_HUMAN PP1A_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. 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~~. ~~Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage~~. ~~Regulator~~ of ~~neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development~~.<~~ref~~>~~PMID:17283141~~</~~ref~~> [[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.<ref>PMID:15084261</ref>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3n5u]] is a 3 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=3N5U OCA].	+

	==See Also==		==See Also==
		+	*[[Protein phosphatase\|Protein phosphatase]]
		+	*[[Serine/threonine protein phosphatase\|Serine/threonine protein phosphatase]]
	*[[User:Iris To/Retinoblastoma Protein Regulation\|User:Iris To/Retinoblastoma Protein Regulation]]		*[[User:Iris To/Retinoblastoma Protein Regulation\|User:Iris To/Retinoblastoma Protein Regulation]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020694007</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
-	[[Category: Cecchini, M.]]	+	[[Category: Cecchini, M]]
-	[[Category: Dick, F A.]]	+	[[Category: Dick, F A]]
-	[[Category: Hirschi, A M.]]	+	[[Category: Hirschi, A M]]
-	[[Category: Rubin, S M.]]	+	[[Category: Rubin, S M]]
-	[[Category: Steinhardt, R C.]]	+	[[Category: Steinhardt, R C]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Phosphatase]]		[[Category: Phosphatase]]

OCA at 18:19, 24 March 2013

2013-03-24T18:19:18Z

←Older revision		Revision as of 18:19, 24 March 2013
Line 2:		Line 2:
	===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===		===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===
	{{ABSTRACT_PUBMED_20694007}}		{{ABSTRACT_PUBMED_20694007}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Defects in RB1 are the cause of childhood cancer retinoblastoma (RB) [MIM:[http://omim.org/entry/180200 180200]]. RB is a congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated.<ref>PMID:2594029</ref><ref>PMID:1352883</ref><ref>PMID:8346255</ref><ref>PMID:7704558</ref><ref>PMID:7927327</ref><ref>PMID:8605116</ref><ref>PMID:7795591</ref><ref>PMID:8776589</ref><ref>PMID:9311732</ref><ref>PMID:9140452</ref><ref>PMID:10671068</ref><ref>PMID:9973307</ref><ref>PMID:11524739</ref> Defects in RB1 are a cause of susceptibility to bladder cancer (BLC) [MIM:[http://omim.org/entry/109800 109800]]. A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in RB1 are a cause of osteogenic sarcoma (OSRC) [MIM:[http://omim.org/entry/259500 259500]].
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref> [[http://www.uniprot.org/uniprot/RB_HUMAN RB_HUMAN]] Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.<ref>PMID:15084261</ref>

	==About this Structure==		==About this Structure==
Line 10:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020694007</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020694007</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]

OCA: Protected "3n5u" [edit=sysop:move=sysop]

2013-03-11T09:12:47Z

Protected "3n5u" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:12, 11 March 2013

OCA at 09:12, 11 March 2013

2013-03-11T09:12:44Z

←Older revision		Revision as of 09:12, 11 March 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:3n5u.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3n5u", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3n5u\| PDB=3n5u \| SCENE= }}		{{STRUCTURE_3n5u\| PDB=3n5u \| SCENE= }}
-
	===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===		===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20694007}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20694007 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20694007}}		{{ABSTRACT_PUBMED_20694007}}

	==About this Structure==		==About this Structure==
-	~~3N5U~~ is a 3 ~~chains~~ structure with ~~sequences~~ 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=3N5U OCA].	+	[[3n5u]] is a 3 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=3N5U OCA].
		+
		+	==See Also==
		+	*[[User:Iris To/Retinoblastoma Protein Regulation\|User:Iris To/Retinoblastoma Protein Regulation]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20694007~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020694007</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
Line 39:		Line 26:
	[[Category: Retinoblastoma]]		[[Category: Retinoblastoma]]
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:23:16 2010''

OCA at 07:14, 15 September 2010

2010-09-15T07:14:35Z

←Older revision		Revision as of 07:14, 15 September 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3n5u.~~jpg~~\|left\|200px]]	+	[[Image:3n5u.png\|left\|200px]]

	<!--		<!--
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	===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===		===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20694007}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20694007 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20694007}}

	==About this Structure==		==About this Structure==
	3N5U is a 3 chains structure with sequences 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=3N5U OCA].		3N5U is a 3 chains structure with sequences 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=3N5U OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20694007</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
Line 31:		Line 40:
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Aug 11~~ 23:~~58:23~~ 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:23:16 2010''

OCA at 19:51, 11 August 2010

2010-08-11T19:51:06Z

←Older revision		Revision as of 19:51, 11 August 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3n5u.jpg\|left\|200px]]

-	The ~~entry 3n5u~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3n5u", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3n5u\| PDB=3n5u \| SCENE= }}

-	~~Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.~~C~~., Dick, F.A., Rubin, S.M.~~	+	===Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1===

-	Description: Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug ~~4 08~~:47:12 2010''	+	==About this Structure==
		+	3N5U is a 3 chains structure with sequences 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=3N5U OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Phosphoprotein phosphatase]]
		+	[[Category: Cecchini, M.]]
		+	[[Category: Dick, F A.]]
		+	[[Category: Hirschi, A M.]]
		+	[[Category: Rubin, S M.]]
		+	[[Category: Steinhardt, R C.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Phosphatase]]
		+	[[Category: Pp1]]
		+	[[Category: Prb]]
		+	[[Category: Protein phosphatase-1]]
		+	[[Category: Rb]]
		+	[[Category: Retinoblastoma]]
		+	[[Category: Transcription regulation]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 11 23:58:23 2010''

OCA at 04:40, 4 August 2010

2010-08-04T04:40:13Z

←Older revision		Revision as of 04:40, 4 August 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3n5u is ON HOLD	+	The entry 3n5u is ON HOLD until Paper Publication

	Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.C., Dick, F.A., Rubin, S.M.		Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.C., Dick, F.A., Rubin, S.M.
Line 7:		Line 7:
	Description: Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1		Description: Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jun~~ 2 08:29:14 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 4 08:47:12 2010''

OCA: New page: '''Unreleased structure''' The entry 3n5u is ON HOLD Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.C., Dick, F.A., Rubin, S.M. Description: Crystal structure of an Rb C-terminal ...

2010-06-02T04:24:46Z

New page: '''Unreleased structure''' The entry 3n5u is ON HOLD Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.C., Dick, F.A., Rubin, S.M. Description: Crystal structure of an Rb C-terminal ...

New page

'''Unreleased structure'''

The entry 3n5u is ON HOLD

Authors: Hirschi, A.M., Cecchini, M., Steinhardt, R.C., Dick, F.A., Rubin, S.M.

Description: Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:29:14 2010''