3oxq - Revision history

OCA at 09:45, 6 September 2023

OCA — Wed, 06 Sep 2023 09:45:32 GMT

←Older revision		Revision as of 09:45, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3oxq' size='340' side='right'caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='3oxq' size='340' side='right'caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oxq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.55Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([https~~:/~~/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=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [https://pdbe.org/3oxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [https://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [https://pdbe.org/3oxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [https://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/~~CAC1C_HUMAN CAC1C_HUMAN~~]~~] Defects~~ in ~~CACNA1C are the cause of Timothy syndrome (TS) [MIM:[https://omim.org/~~entry~~/601005 601005]]~~. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref> <ref>PMID:15863612</ref> Defects in ~~CACNA1C~~ are the cause of ~~Brugada syndrome type 3 (BRGDA3) [MIM:[https://omim~~.~~org/entry/611875 611875]]. A heart~~ disease ~~characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome~~ is ~~a tachyarrhythmia characterized~~ by ~~right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause~~ the ~~ventricles to beat so fast that the blood is prevented from circulating efficiently~~ in ~~the body~~. ~~When this situation occurs (called ventricular fibrillation), the individual will faint and may die~~ in ~~a few minutes if~~ the ~~heart is not reset~~.~~<ref>PMID:17224476</ref>~~	+	[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CAC1C_HUMAN CAC1C_HUMAN~~]~~] Voltage-sensitive calcium channels (VSCC) mediate~~ the ~~entry~~ of ~~calcium ions into excitable cells and are also involved in~~ a ~~variety~~ of ~~calcium-dependent processes~~, ~~including muscle contraction~~, ~~hormone or neurotransmitter release, gene expression, cell motility, cell division~~ and ~~cell death. The isoform alpha~~-~~1C gives rise to L-type calcium currents~~. ~~Long-lasting (L-type) calcium channels belong~~ to the ~~'high~~-~~voltage activated' (HVA) group~~. ~~They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines~~, and ~~by omega-agatoxin-IIIA~~ (~~omega-Aga-IIIA~~). ~~They are however insensitive to omega~~-~~conotoxin-GVIA~~ (~~omega-CTx-GVIA~~) ~~and omega~~-~~agatoxin-IVA~~ (~~omega-Aga-IVA~~). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref> <ref>PMID:7737988</ref> <ref>PMID:~~9013606~~</ref> <ref>PMID:~~9607315~~</ref> <ref>PMID:~~12176756~~</ref> <ref>PMID:~~17071743~~</ref>	+	[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arant, R]]	+	[[Category: Arant R]]
-	[[Category: Cooley~~, E S~~]]	+	[[Category: Cooley ES]]
-	[[Category: Findeisen, F]]	+	[[Category: Findeisen F]]
-	[[Category: Isacoff~~, E Y~~]]	+	[[Category: Isacoff EY]]
-	[[Category: Kim~~, E Y~~]]	+	[[Category: Kim EY]]
-	[[Category: Minor~~, D L]]~~	+	[[Category: Minor DL]]
-	~~[[Category: Petegem, F Van~~]]	+	[[Category: Rumpf CH]]
-	[[Category: Rumpf~~, C H~~]]	+	[[Category: Van Petegem F]]
-	[[Category: ~~Calcium binding]]~~	+
-	~~[[Category: Calcium sensing]]~~	+
-	~~[[Category: Ef hand iq domain]]~~	+
-	~~[[Category: Ion channel]]~~	+
-	~~[[Category: Metal binding protein-transport protein complex~~]]	+

OCA at 11:02, 18 May 2022

OCA — Wed, 18 May 2022 11:02:07 GMT

←Older revision		Revision as of 11:02, 18 May 2022
Line 1:		Line 1:

	==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==		==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==
-	<StructureSection load='3oxq' size='340' side='right' caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>	+	<StructureSection load='3oxq' size='340' side='right'caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oxq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([https://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=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [~~http~~://pdbe.org/3oxq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [https://pdbe.org/3oxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [https://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:[~~http~~://omim.org/entry/601005 601005]]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref> <ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[~~http~~://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:17224476</ref>	+	[[https://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:[https://omim.org/entry/601005 601005]]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref> <ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[https://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:17224476</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref> <ref>PMID:7737988</ref> <ref>PMID:9013606</ref> <ref>PMID:9607315</ref> <ref>PMID:12176756</ref> <ref>PMID:17071743</ref>	+	[[https://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref> <ref>PMID:7737988</ref> <ref>PMID:9013606</ref> <ref>PMID:9607315</ref> <ref>PMID:12176756</ref> <ref>PMID:17071743</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Calmodulin\|Calmodulin]]	+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	*[[Ion channels\|Ion channels]]	+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arant, R]]		[[Category: Arant, R]]
	[[Category: Cooley, E S]]		[[Category: Cooley, E S]]

OCA at 11:10, 5 August 2016

OCA — Fri, 05 Aug 2016 11:10:25 GMT

←Older revision		Revision as of 11:10, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==		==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==
	<StructureSection load='3oxq' size='340' side='right' caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='3oxq' size='340' side='right' caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([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">CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([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=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [http://www.ebi.ac.uk/pdbsum/3oxq 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=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [http://pdbe.org/3oxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [http://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 3oxq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Arant, R]]		[[Category: Arant, R]]
	[[Category: Cooley, E S]]		[[Category: Cooley, E S]]

OCA at 07:00, 19 December 2014

OCA — Fri, 19 Dec 2014 07:00:12 GMT

←Older revision		Revision as of 07:00, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3oxq\| PDB=3oxq \| SCENE= }}~~	+	==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==
-	===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===	+	<StructureSection load='3oxq' size='340' side='right' caption='[[3oxq]], [[Resolution\|resolution]] 2.55Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20953164}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OXQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CALM, CALM1, CALM2, CALM3, CALML2, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [http://www.ebi.ac.uk/pdbsum/3oxq PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:[http://omim.org/entry/601005 601005]]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref> <ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[http://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:17224476</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref> <ref>PMID:7737988</ref> <ref>PMID:9013606</ref> <ref>PMID:9607315</ref> <ref>PMID:12176756</ref> <ref>PMID:17071743</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Interactions between voltage-gated calcium channels (Ca(V)s) and calmodulin (CaM) modulate Ca(V) function. In this study, we report the structure of a Ca(2+)/CaM Ca(V)1.2 C-terminal tail complex that contains two PreIQ helices bridged by two Ca(2+)/CaMs and two Ca(2+)/CaM-IQ domain complexes. Sedimentation equilibrium experiments establish that the complex has a 2:1 Ca(2+)/CaM:C-terminal tail stoichiometry and does not form higher order assemblies. Moreover, subunit-counting experiments demonstrate that in live cell membranes Ca(V)1.2s are monomers. Thus, contrary to previous proposals, the crystallographic dimer lacks physiological relevance. Isothermal titration calorimetry and biochemical experiments show that the two Ca(2+)/CaMs in the complex have different properties. Ca(2+)/CaM bound to the PreIQ C-region is labile, whereas Ca(2+)/CaM bound to the IQ domain is not. Furthermore, neither of lobes of apo-CaM interacts strongly with the PreIQ domain. Electrophysiological studies indicate that the PreIQ C-region has a role in calcium-dependent facilitation. Together, the data show that two Ca(2+)/CaMs can bind the Ca(V)1.2 tail simultaneously and indicate a functional role for Ca(2+)/CaM at the C-region site.

-	~~==Disease==~~	+	Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.,Kim EY, Rumpf CH, Van Petegem F, Arant RJ, Findeisen F, Cooley ES, Isacoff EY, Minor DL Jr EMBO J. 2010 Oct 15. PMID:20953164<ref>PMID:20953164</ref>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome~~ (TS) ~~[MIM:[http://omim~~.~~org/entry/601005 601005]]~~. ~~TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias~~, ~~webbing of fingers and toes~~, ~~congenital heart disease~~, ~~immune deficiency~~, ~~intermittent hypoglycemia~~, ~~cognitive abnormalities and autism~~.~~<ref>~~PMID:15454078</ref><ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[http://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:~~17224476~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in~~ a ~~variety~~ of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the ~~'high-voltage activated' (HVA) group~~. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. ~~Binding~~ of ~~calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function~~.<~~ref~~>~~PMID:8392192~~</~~ref~~>~~<ref>PMID:7737988</ref><ref>PMID:9013606</ref><ref>PMID:9607315</ref><ref>PMID:12176756</ref><ref>PMID:17071743</ref>~~	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3oxq]] is a 6 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=3OXQ OCA].	+

	==See Also==		==See Also==
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
	*[[Ion channels\|Ion channels]]		*[[Ion channels\|Ion channels]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020953164</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Arant, R.]]	+	[[Category: Arant, R]]
-	[[Category: Cooley, E S.]]	+	[[Category: Cooley, E S]]
-	[[Category: Findeisen, F.]]	+	[[Category: Findeisen, F]]
-	[[Category: Isacoff, E Y.]]	+	[[Category: Isacoff, E Y]]
-	[[Category: Kim, E Y.]]	+	[[Category: Kim, E Y]]
-	[[Category: Minor, D L.]]	+	[[Category: Minor, D L]]
-	[[Category: Petegem, F Van.]]	+	[[Category: Petegem, F Van]]
-	[[Category: Rumpf, C H.]]	+	[[Category: Rumpf, C H]]
	[[Category: Calcium binding]]		[[Category: Calcium binding]]
	[[Category: Calcium sensing]]		[[Category: Calcium sensing]]

OCA at 21:00, 24 March 2013

OCA — Sun, 24 Mar 2013 21:00:37 GMT

←Older revision		Revision as of 21:00, 24 March 2013
Line 1:		Line 1:
-	[[Image:3oxq.png\|left\|200px]]
-
	{{STRUCTURE_3oxq\| PDB=3oxq \| SCENE= }}		{{STRUCTURE_3oxq\| PDB=3oxq \| SCENE= }}
-
	===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===		===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===
		+	{{ABSTRACT_PUBMED_20953164}}

-	~~{{ABSTRACT_PUBMED_20953164}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:[http://omim.org/entry/601005 601005]]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref><ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[http://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:17224476</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref><ref>PMID:7737988</ref><ref>PMID:9013606</ref><ref>PMID:9607315</ref><ref>PMID:12176756</ref><ref>PMID:17071743</ref>

	==About this Structure==		==About this Structure==
Line 15:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020953164</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020953164</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Arant, R.]]		[[Category: Arant, R.]]

OCA at 19:53, 20 October 2012

OCA — Sat, 20 Oct 2012 19:53:55 GMT

←Older revision		Revision as of 19:53, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3oxq]] is a 6 chain structure ~~of [[]], [[Calmodulin]] and [[Ion channels]]~~ 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=3OXQ OCA].	+	[[3oxq]] is a 6 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=3OXQ OCA].

	==See Also==		==See Also==
-	*[[\|]]
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
	*[[Ion channels\|Ion channels]]		*[[Ion channels\|Ion channels]]

OCA at 18:51, 6 August 2012

OCA — Mon, 06 Aug 2012 18:51:47 GMT

←Older revision		Revision as of 18:51, 6 August 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3oxq]] is a 6 chain structure of [[~~Calmodulin~~]], [[~~Ion channels~~]] and [[Ion channels ~~(Part II)~~]] 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=3OXQ OCA].	+	[[3oxq]] is a 6 chain structure of [[]], [[Calmodulin]] and [[Ion channels]] 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=3OXQ OCA].

	==See Also==		==See Also==
		+	*[[\|]]
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
	*[[Ion channels\|Ion channels]]		*[[Ion channels\|Ion channels]]
-	*[[Ion channels (Part II)\|Ion channels (Part II)]]

	==Reference==		==Reference==

OCA at 08:49, 27 July 2012

OCA — Fri, 27 Jul 2012 08:49:37 GMT

←Older revision		Revision as of 08:49, 27 July 2012
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	[[Image:3oxq.png\|left\|200px]]		[[Image:3oxq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3oxq", 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_3oxq\| PDB=3oxq \| SCENE= }}		{{STRUCTURE_3oxq\| PDB=3oxq \| SCENE= }}

	===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===		===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20953164}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20953164 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20953164}}		{{ABSTRACT_PUBMED_20953164}}

	==About this Structure==		==About this Structure==
-	[[3oxq]] is a 6 chain structure of [[Ion channels]] and [[Ion channels (Part II)]] 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=3OXQ OCA].	+	[[3oxq]] is a 6 chain structure of [[Calmodulin]], [[Ion channels]] and [[Ion channels (Part II)]] 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=3OXQ OCA].

	==See Also==		==See Also==
-	*[[Ion channels]]	+	*[[Calmodulin\|Calmodulin]]
-	*[[Ion channels (Part II)]]	+	*[[Ion channels\|Ion channels]]
		+	*[[Ion channels (Part II)\|Ion channels (Part II)]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20953164~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020953164</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Arant, R.]]		[[Category: Arant, R.]]
Line 36:		Line 26:
	[[Category: Petegem, F Van.]]		[[Category: Petegem, F Van.]]
	[[Category: Rumpf, C H.]]		[[Category: Rumpf, C H.]]
		+	[[Category: Calcium binding]]
		+	[[Category: Calcium sensing]]
		+	[[Category: Ef hand iq domain]]
		+	[[Category: Ion channel]]
		+	[[Category: Metal binding protein-transport protein complex]]

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

OCA — Wed, 06 Apr 2011 08:06:02 GMT

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

←Older revision

Revision as of 08:06, 6 April 2011

OCA at 08:06, 6 April 2011

OCA — Wed, 06 Apr 2011 08:06:00 GMT

←Older revision		Revision as of 08:06, 6 April 2011
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-	~~{{Seed}}~~	+	[[Image:3oxq.png\|left\|200px]]
-	[[Image:3oxq.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	==About this Structure==		==About this Structure==
-	~~3OXQ~~ is a 6 ~~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=3OXQ OCA].	+	[[3oxq]] is a 6 chain structure of [[Ion channels]] and [[Ion channels (Part II)]] 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=3OXQ OCA].
		+
		+	==See Also==
		+	*[[Ion channels]]
		+	*[[Ion channels (Part II)]]

	==Reference==		==Reference==
Line 33:		Line 36:
	[[Category: Petegem, F Van.]]		[[Category: Petegem, F Van.]]
	[[Category: Rumpf, C H.]]		[[Category: Rumpf, C H.]]
-	[[Category: Calcium binding]]
-	[[Category: Calcium sensing]]
-	[[Category: Ef hand iq domain]]
-	[[Category: Ion channel]]
-	[[Category: Metal binding protein-transport protein complex]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 3 11:14:16 2010''