5k6p - Revision history

OCA at 10:12, 14 June 2023

2023-06-14T10:12:46Z

←Older revision		Revision as of 10:12, 14 June 2023
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	==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==		==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==
-	<StructureSection load='5k6p' size='340' side='right'caption='[[5k6p~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='5k6p' size='340' side='right'caption='[[5k6p]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k6p]] 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=5K6P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5K6P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k6p]] 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=5K6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K6P FirstGlance]. <br>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MYBPC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [https://pdbe.org/5k6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [https://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p 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=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [~~http~~://pdbe.org/5k6p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Defects in MYBPC3 are the cause of familial hypertrophic cardiomyopathy type 4 (CMH4) [MIM:[~~http~~://omim.org/entry/115197 115197]]. Familial hypertrophic cardiomyopathy 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:7744002</ref> <ref>PMID:9048664</ref> <ref>PMID:9562578</ref> <ref>PMID:9541104</ref> <ref>PMID:9541115</ref> <ref>PMID:11499718</ref> <ref>PMID:11499719</ref> <ref>PMID:12379228</ref> <ref>PMID:11815426</ref> <ref>PMID:12951062</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:14563344</ref> <ref>PMID:12628722</ref> <ref>PMID:12818575</ref> <ref>PMID:15114369</ref> <ref>PMID:15519027</ref> <ref>PMID:15563892</ref> <ref>PMID:16199542</ref> <ref>PMID:18403758</ref>	+	[https://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN] Defects in MYBPC3 are the cause of familial hypertrophic cardiomyopathy type 4 (CMH4) [MIM:[https://omim.org/entry/115197 115197]. Familial hypertrophic cardiomyopathy 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:7744002</ref> <ref>PMID:9048664</ref> <ref>PMID:9562578</ref> <ref>PMID:9541104</ref> <ref>PMID:9541115</ref> <ref>PMID:11499718</ref> <ref>PMID:11499719</ref> <ref>PMID:12379228</ref> <ref>PMID:11815426</ref> <ref>PMID:12951062</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:14563344</ref> <ref>PMID:12628722</ref> <ref>PMID:12818575</ref> <ref>PMID:15114369</ref> <ref>PMID:15519027</ref> <ref>PMID:15563892</ref> <ref>PMID:16199542</ref> <ref>PMID:18403758</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.	+	[https://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN] Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
	<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: Guss~~, J M~~]]	+	[[Category: Guss JM]]
-	[[Category: Kwan~~, A H~~]]	+	[[Category: Kwan AH]]
-	[[Category: Michie~~, K A~~]]	+	[[Category: Michie KA]]
-	[[Category: Trewhella, J]]	+	[[Category: Trewhella J]]
-	[[Category: Tung~~, C S]]~~	+	[[Category: Tung CS]]
-	~~[[Category: Contractile protein]]~~	+
-	~~[[Category: Immunoglobulin~~]]	+

OCA at 09:00, 1 January 2020

2020-01-01T09:00:35Z

←Older revision		Revision as of 09:00, 1 January 2020
Line 1:		Line 1:

	==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==		==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==
-	<StructureSection load='5k6p' size='340' side='right' caption='[[5k6p]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='5k6p' size='340' side='right'caption='[[5k6p]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5k6p]] 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=5K6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6P FirstGlance]. <br>		<table><tr><td colspan='2'>[[5k6p]] 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=5K6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6P FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Guss, J M]]		[[Category: Guss, J M]]
	[[Category: Kwan, A H]]		[[Category: Kwan, A H]]

OCA at 06:04, 1 November 2017

2017-11-01T06:04:26Z

←Older revision		Revision as of 06:04, 1 November 2017
Line 3:		Line 3:
	<StructureSection load='5k6p' size='340' side='right' caption='[[5k6p]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='5k6p' size='340' side='right' caption='[[5k6p]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k6p]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k6p]] 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=5K6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6P 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=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [http://pdbe.org/5k6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [http://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MYBPC3 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [http://pdbe.org/5k6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [http://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Guss, J M]]		[[Category: Guss, J M]]
	[[Category: Kwan, A H]]		[[Category: Kwan, A H]]

OCA at 19:52, 9 December 2016

2016-12-09T19:52:17Z

←Older revision		Revision as of 19:52, 9 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5k6p is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==
		+	<StructureSection load='5k6p' size='340' side='right' caption='[[5k6p]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5k6p]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6P 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=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [http://pdbe.org/5k6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [http://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Defects in MYBPC3 are the cause of familial hypertrophic cardiomyopathy type 4 (CMH4) [MIM:[http://omim.org/entry/115197 115197]]. Familial hypertrophic cardiomyopathy 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:7744002</ref> <ref>PMID:9048664</ref> <ref>PMID:9562578</ref> <ref>PMID:9541104</ref> <ref>PMID:9541115</ref> <ref>PMID:11499718</ref> <ref>PMID:11499719</ref> <ref>PMID:12379228</ref> <ref>PMID:11815426</ref> <ref>PMID:12951062</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:14563344</ref> <ref>PMID:12628722</ref> <ref>PMID:12818575</ref> <ref>PMID:15114369</ref> <ref>PMID:15519027</ref> <ref>PMID:15563892</ref> <ref>PMID:16199542</ref> <ref>PMID:18403758</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The nuclear magnetic resonance (NMR) structure of the tri-helix bundle (THB) of the m-domain plus C2 (DeltamC2) of myosin-binding protein C (MyBP-C) has revealed a highly flexible seven-residue linker between the structured THB and C2. Bioinformatics shows significant patterns of conservation across the THB-linker sequence, with the linker containing a strictly conserved serine in all MyBP-C isoforms. Clinically linked mutations further support the functional significance of the THB-linker region. NMR, small-angle X-ray scattering, and binding studies show the THB-linker plus the first ten residues of C2 undergo dramatic changes when DeltamC2 binds Ca2+-calmodulin, with the linker and C2 N-terminal residues contributing significantly to the affinity. Modeling of all available experimental data indicates that the THB tertiary structure must be disrupted to form the complex. These results are discussed in the context of the THB-linker and the N-terminal residues of C2 forming a polymorphic binding domain that could accommodate multiple binding partners in the dynamic sarcomere.

-	~~Authors~~:	+	A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C.,Michie KA, Kwan AH, Tung CS, Guss JM, Trewhella J Structure. 2016 Nov 1;24(11):2000-2007. doi: 10.1016/j.str.2016.08.018. Epub 2016, Oct 6. PMID:27720588<ref>PMID:27720588</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5k6p" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Guss, J M]]
		+	[[Category: Kwan, A H]]
		+	[[Category: Michie, K A]]
		+	[[Category: Trewhella, J]]
		+	[[Category: Tung, C S]]
		+	[[Category: Contractile protein]]
		+	[[Category: Immunoglobulin]]

OCA at 00:03, 13 July 2016

2016-07-13T00:03:43Z

←Older revision		Revision as of 00:03, 13 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5k6p is ON HOLD	+	The entry 5k6p is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5k6p" [edit=sysop:move=sysop]

2016-06-01T14:23:52Z

Protected "5k6p" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:23, 1 June 2016

OCA: New page: '''Unreleased structure''' The entry 5k6p is ON HOLD Authors: Description: Category: Unreleased Structures

2016-06-01T14:23:50Z

New page: '''Unreleased structure''' The entry 5k6p is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5k6p is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]