1plp - Revision history

OCA at 18:56, 29 November 2023

2023-11-29T18:56:03Z

←Older revision		Revision as of 18:56, 29 November 2023
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	==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==		==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==
-	<StructureSection load='1plp' size='340' side='right'caption='[[1plp~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1plp' size='340' side='right'caption='[[1plp]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
-	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [https://pdbe.org/1plp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [https://www.ebi.ac.uk/pdbsum/1plp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plp ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [https://pdbe.org/1plp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [https://www.ebi.ac.uk/pdbsum/1plp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[https://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref> <ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[https://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>	+	[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[https://omim.org/entry/609909 609909]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref> <ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[https://omim.org/entry/613874 613874]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.	+	[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Burke~~, C J~~]]	+	[[Category: Burke CJ]]
-	[[Category: Garsky~~, V M~~]]	+	[[Category: Garsky VM]]
-	[[Category: Johnson~~, R G~~]]	+	[[Category: Johnson RG]]
-	[[Category: Middaugh~~, C R~~]]	+	[[Category: Middaugh CR]]
-	[[Category: Mortishire-Smith~~, R J~~]]	+	[[Category: Mortishire-Smith RJ]]
-	[[Category: Pitzenberger~~, S M]]~~	+	[[Category: Pitzenberger SM]]
-	~~[[Category: Atpase]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Phospholamban]]~~	+
-	~~[[Category: Phosphorylation~~]]	+

OCA at 09:31, 8 September 2021

2021-09-08T09:31:40Z

←Older revision		Revision as of 09:31, 8 September 2021
Line 3:		Line 3:
	<StructureSection load='1plp' size='340' side='right'caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1plp' size='340' side='right'caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
-	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [~~http~~://pdbe.org/1plp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1plp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1plp ProSAT]</span></td></tr>	+	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [https://pdbe.org/1plp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [https://www.ebi.ac.uk/pdbsum/1plp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[~~http~~://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref> <ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[~~http~~://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>	+	[[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[https://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref> <ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[https://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.	+	[[https://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:20, 27 November 2019

2019-11-27T10:20:00Z

←Older revision		Revision as of 10:20, 27 November 2019
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==		==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==
-	<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1plp' size='340' side='right'caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 1plp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1plp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phospholamban\|Phospholamban]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Burke, C J]]		[[Category: Burke, C J]]
	[[Category: Garsky, V M]]		[[Category: Garsky, V M]]

OCA at 08:20, 24 February 2018

2018-02-24T08:20:05Z

←Older revision		Revision as of 08:20, 24 February 2018
Line 1:		Line 1:
		+
	==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==		==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==
	<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
-	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [http://pdbe.org/1plp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [http://www.ebi.ac.uk/pdbsum/1plp PDBsum]</span></td></tr>	+	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [http://pdbe.org/1plp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [http://www.ebi.ac.uk/pdbsum/1plp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1plp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 1plp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1plp" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Phospholamban\|Phospholamban]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:53, 11 September 2015

2015-09-11T10:53:47Z

←Older revision		Revision as of 10:53, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
-	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [http://www.ebi.ac.uk/pdbsum/1plp PDBsum]</span></td></tr>	+	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [http://pdbe.org/1plp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [http://www.ebi.ac.uk/pdbsum/1plp PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 17:
	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 1plp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phospholamban\|Phospholamban]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Burke, C J]]		[[Category: Burke, C J]]
	[[Category: Garsky, V M]]		[[Category: Garsky, V M]]

OCA at 12:33, 18 December 2014

2014-12-18T12:33:05Z

←Older revision		Revision as of 12:33, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}~~	+	==SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN==
-	===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===	+	<StructureSection load='1plp' size='340' side='right' caption='[[1plp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_7779806}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PLP FirstGlance]. <br>
-	==Disease==	+	</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=1plp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1plp RCSB], [http://www.ebi.ac.uk/pdbsum/1plp PDBsum]</span></td></tr>
-	[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[http://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref><ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[http://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>	+	</table>
-		+	== Disease ==
-	==Function==	+	[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[http://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref> <ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[http://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.		[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peptides representing the N-terminal domain (Ia) of the cardiac sarcoplasmic reticulum protein phospholamban (residues 1-25 [PLB(1-25)] and a phosphorylated form [pPLB(1-25)]) were synthesized and their conformations examined using circular dichroism and nuclear magnetic resonance spectroscopy. In aqueous solution, both PLB(1-25) and pPLB(1-25) adopt a primarily disordered conformation. In 30% trifluoroethanol/10 mM phosphate, PLB(1-25) exhibits a CD spectrum consistent with 60% helical structure. This value decreases to 27% for the phosphorylated peptide. CD spectra in 2% SDS indicate 40% alpha-helix for PLB(1-25) and 20% for pPLB(1-25). Full chemical shift assignments were obtained by conventional homonuclear NMR methodologies for both PLB(1-25) and pPLB(1-25) in 30% trifluoroethanol/water and 300 mM SDS. The solution structure of PLB(1-25) in 30% TFE/water was determined from distance geometry calculations using 54 NOE distance constraints and 17 torsion angle constraints. In the family of 20 calculated conformers, the root mean square deviation from the mean structure is 0.79 A for backbone heavy atoms of residues 1-17. The structure comprises a regular alpha-helix extending from M1 to S16 with the remaining C-terminal residues disordered. The calculated structure is supported by analysis of C alpha H secondary shifts which are significantly negative for residues 1-16. Chemical shift degeneracy is substantially more extensive in the phospho form and precludes a direct comparison of calculated structures. However, the magnitudes of upfield secondary shifts are decreased by 20% in residues 1-11 and are not significantly helical for residues 12-16 according to the criteria of Wishart et al. [(1992) Biochemistry 31, 1647-1651]. 3JHN alpha coupling constants measured for I12, R13, A15, and S16 also suggest that residues 12-16 undergo a local unwinding of the helix upon phosphorylation. Similar results are obtained for PLB(1-25) and pPLB(1-25) in 300 mM perdeuterated sodium dodecyl sulfate except that differences in backbone dynamics for the helical and nonhelical regions of the peptide are evident in the DQF-COSY line shapes for fingerprint cross-peaks. This disruption of structure at the C-terminus of the helix suggests a model for phosphorylation-induced dissociation of the PLB/Ca(2+)-ATPase complex.

-	~~==About this Structure==~~	+	Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure.,Mortishire-Smith RJ, Pitzenberger SM, Burke CJ, Middaugh CR, Garsky VM, Johnson RG Biochemistry. 1995 Jun 13;34(23):7603-13. PMID:7779806<ref>PMID:7779806</ref>
-	~~[[1plp]] is~~ a ~~1 chain~~ structure ~~with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full experimental information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:007779806</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Burke, C J.]]	+	[[Category: Burke, C J]]
-	[[Category: Garsky, V M.]]	+	[[Category: Garsky, V M]]
-	[[Category: Johnson, R G.]]	+	[[Category: Johnson, R G]]
-	[[Category: Middaugh, C R.]]	+	[[Category: Middaugh, C R]]
-	[[Category: Mortishire-Smith, R J.]]	+	[[Category: Mortishire-Smith, R J]]
-	[[Category: Pitzenberger, S M.]]	+	[[Category: Pitzenberger, S M]]
	[[Category: Atpase]]		[[Category: Atpase]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
	[[Category: Phospholamban]]		[[Category: Phospholamban]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]

OCA at 10:05, 24 March 2013

2013-03-24T10:05:17Z

←Older revision		Revision as of 10:05, 24 March 2013
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-	[[Image:1plp.png\|left\|200px]]
-
	{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}		{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}
-
	===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===		===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===
		+	{{ABSTRACT_PUBMED_7779806}}

-	~~{{ABSTRACT_PUBMED_7779806}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Defects in PLN are the cause of cardiomyopathy dilated type 1P (CMD1P) [MIM:[http://omim.org/entry/609909 609909]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:12610310</ref><ref>PMID:16432188</ref> Defects in PLN are the cause of familial hypertrophic cardiomyopathy type 18 (CMH18) [MIM:[http://omim.org/entry/613874 613874]]. CMH18 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:12705874</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/PPLA_HUMAN PPLA_HUMAN]] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:007779806</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007779806</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burke, C J.]]		[[Category: Burke, C J.]]

OCA: Protected "1plp" [edit=sysop:move=sysop]

2012-08-14T16:12:51Z

Protected "1plp" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:12, 14 August 2012

OCA at 16:12, 14 August 2012

2012-08-14T16:12:49Z

←Older revision		Revision as of 16:12, 14 August 2012
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-	{{Seed}}
	[[Image:1plp.png\|left\|200px]]		[[Image:1plp.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1plp", 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_1plp\| PDB=1plp \| SCENE= }}		{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}

	===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===		===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_7779806}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 7779806 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_7779806}}		{{ABSTRACT_PUBMED_7779806}}

	==About this Structure==		==About this Structure==
-	~~1PLP is a~~ [[~~Single protein~~]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA].	+	[[1plp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA].

	==Reference==		==Reference==
-	Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure., Mortishire-Smith RJ, Pitzenberger SM, Burke CJ, Middaugh CR, Garsky VM, Johnson RG, Biochemistry. 1995 Jun 13;34(23):7603-13. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~7779806 7779806]~~	+	<ref group="xtra">PMID:007779806</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Burke, C J.]]		[[Category: Burke, C J.]]
	[[Category: Garsky, V M.]]		[[Category: Garsky, V M.]]
Line 33:		Line 20:
	[[Category: Pitzenberger, S M.]]		[[Category: Pitzenberger, S M.]]
	[[Category: Atpase]]		[[Category: Atpase]]
		+	[[Category: Membrane protein]]
	[[Category: Phospholamban]]		[[Category: Phospholamban]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:15:26 2008''

OCA at 01:15, 29 July 2008

2008-07-29T01:15:28Z

←Older revision		Revision as of 01:15, 29 July 2008
Line 1:		Line 1:
-	[[Image:1plp.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1plp.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}		{{STRUCTURE_1plp\| PDB=1plp \| SCENE= }}

-	~~'''~~SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN~~'''~~	+	===SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN===


-	~~==Overview==~~	+	<!--
-	~~Peptides representing the N~~-~~terminal domain (Ia) of the cardiac sarcoplasmic reticulum protein phospholamban (residues 1~~-~~25 [PLB(1-25)] and a phosphorylated form [pPLB(1-25)]) were synthesized and their conformations examined using circular dichroism and nuclear magnetic resonance spectroscopy. In aqueous solution~~, ~~both PLB(1-25) and pPLB(1-25) adopt a primarily disordered conformation. In 30% trifluoroethanol/10 mM phosphate~~, ~~PLB(1-25) exhibits a CD spectrum consistent with 60% helical structure. This value decreases~~ to ~~27% for~~ the ~~phosphorylated peptide. CD spectra in 2% SDS indicate 40% alpha-helix for PLB~~(~~1-25) and 20% for pPLB(1-25). Full chemical shift assignments were obtained by conventional homonuclear NMR methodologies for both PLB(1-25) and pPLB(1-25) in 30% trifluoroethanol~~/~~water and 300 mM SDS. The solution structure of PLB(1-25) in 30% TFE~~/~~water was determined from distance geometry calculations using 54 NOE distance constraints and 17 torsion angle constraints~~. ~~In the family of 20 calculated conformers, the root mean square deviation from the mean structure is 0~~.79 A for backbone heavy atoms of residues 1-17. The structure comprises a regular alpha-helix extending from M1 to S16 with the remaining C-terminal residues disordered. The calculated structure is supported by analysis of C alpha H secondary shifts which are significantly negative for residues 1-16. Chemical shift degeneracy is substantially more extensive in the phospho form and precludes a direct comparison of calculated structures. However, the magnitudes of upfield secondary shifts are decreased by 20% in residues 1-11 and are not significantly helical for residues 12-16 according to the criteria of Wishart et al. [(1992) ~~Biochemistry 31~~, ~~1647-1651]. 3JHN alpha coupling constants measured for I12, R13, A15, and S16 also suggest that residues 12-16 undergo a local unwinding of~~ the ~~helix upon phosphorylation~~. ~~Similar results are obtained for PLB(1~~-~~25) and pPLB(1~~-25) in 300 mM perdeuterated sodium dodecyl sulfate except that differences in backbone dynamics for the helical and nonhelical regions of the peptide are evident in the DQF-COSY line shapes for fingerprint cross-peaks. This disruption of structure at the C-terminus of the helix suggests a model for phosphorylation-induced dissociation of the PLB/Ca(2+)-ATPase complex.	+	The line below this paragraph, {{ABSTRACT_PUBMED_7779806}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 7779806 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_7779806}}

	==About this Structure==		==About this Structure==
-	1PLP is a [[Single protein]] structure of 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=1PLP OCA].	+	1PLP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLP OCA].

	==Reference==		==Reference==
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	[[Category: Phospholamban]]		[[Category: Phospholamban]]
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 05~~:13:46 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:15:26 2008''