3bxk - Revision history

OCA at 09:31, 21 February 2024

OCA — Wed, 21 Feb 2024 09:31:34 GMT

←Older revision		Revision as of 09:31, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3bxk' size='340' side='right'caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='3bxk' size='340' side='right'caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXK 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>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3bxl\|3bxl]]~~</~~div~~><~~/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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">Calm1, Calm, Cam, Cam1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])~~</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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [https://pdbe.org/3bxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [https://www.ebi.ac.uk/pdbsum/3bxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxk 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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [https://pdbe.org/3bxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [https://www.ebi.ac.uk/pdbsum/3bxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxk ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[https://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[https://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[https://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CAC1A_HUMAN CAC1A_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~~-~~1A gives rise to P and/or Q-type calcium currents~~. ~~P/Q-type calcium channels belong~~ to the ~~'high~~-~~voltage activated' (HVA) group and~~ are ~~blocked by the funnel toxin (Ftx)~~ and ~~by the omega-agatoxin-IVA (omega-Aga-IVA)~~. ~~They are however insensitive to dihydropyridines (DHP)~~, and ~~omega~~-~~conotoxin~~-~~GVIA (omega-CTx-GVIA)~~.	+	[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] 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. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Kooi, C W.Vander~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Leahy~~, D J~~]]	+	[[Category: Leahy DJ]]
-	[[Category: Mori~~, M X~~]]	+	[[Category: Mori MX]]
-	[[Category: ~~Yue, D T~~]]	+	[[Category: Vander Kooi CW]]
-	[[Category: ~~Acetylation]]~~	+	[[Category: Yue DT]]
-	~~[[Category: Calcium channel]]~~	+
-	~~[[Category: Calcium transport]]~~	+
-	~~[[Category: Calcium-dependent]]~~	+
-	~~[[Category: Calmodulin]]~~	+
-	~~[[Category: Facillitation]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Inactivation]]~~	+
-	~~[[Category: Ion channel]]~~	+
-	~~[[Category: Ion transport]]~~	+
-	~~[[Category: Ionic channel]]~~	+
-	~~[[Category: Iq domain]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Methylation]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Robetta]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Simulation]]~~	+
-	~~[[Category: Transmembrane]]~~	+
-	~~[[Category: Transport]]~~	+
-	~~[[Category: Voltage-gated]]~~	+
-	~~[[Category: Voltage-gated channel~~]]	+

OCA at 08:28, 19 January 2022

OCA — Wed, 19 Jan 2022 08:28:22 GMT

←Older revision		Revision as of 08:28, 19 January 2022
Line 1:		Line 1:

	==Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex==		==Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex==
-	<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>	+	<StructureSection load='3bxk' size='340' side='right'caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3BXK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXK 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bxl\|3bxl]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [~~http~~://pdbe.org/3bxk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3bxk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxk 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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [https://pdbe.org/3bxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [https://www.ebi.ac.uk/pdbsum/3bxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxk ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[~~http~~://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[~~http~~://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[~~http~~://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>	+	[[https://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[https://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[https://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[https://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).	+	[[https://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 25:		Line 25:

	==See Also==		==See Also==
-	*[[Calmodulin\|Calmodulin]]	+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	*[[MoRFs\|MoRFs]]	+
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Kooi, C W.Vander]]		[[Category: Kooi, C W.Vander]]
	[[Category: Leahy, D J]]		[[Category: Leahy, D J]]

OCA at 13:57, 7 November 2018

OCA — Wed, 07 Nov 2018 13:57:05 GMT

←Older revision		Revision as of 13:57, 7 November 2018
Line 1:		Line 1:
		+
	==Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex==		==Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex==
	<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://pdbe.org/3bxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk 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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://pdbe.org/3bxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxk ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/3bxk_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/3bxk_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>

OCA at 03:24, 9 February 2016

OCA — Tue, 09 Feb 2016 03:24:31 GMT

←Older revision		Revision as of 03:24, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXK 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk 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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://pdbe.org/3bxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	<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=3bxk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>

Line 30:		Line 30:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Kooi, C W.Vander]]		[[Category: Kooi, C W.Vander]]
	[[Category: Leahy, D J]]		[[Category: Leahy, D J]]

OCA at 10:49, 20 January 2015

OCA — Tue, 20 Jan 2015 10:49:28 GMT

←Older revision		Revision as of 10:49, 20 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXK FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk 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=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[http://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[http://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[http://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>		[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[http://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[http://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[http://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Kooi, C W.Vander.]]	+	[[Category: Kooi, C W.Vander]]
-	[[Category: Leahy, D J.]]	+	[[Category: Leahy, D J]]
-	[[Category: Mori, M X.]]	+	[[Category: Mori, M X]]
-	[[Category: Yue, D T.]]	+	[[Category: Yue, D T]]
	[[Category: Acetylation]]		[[Category: Acetylation]]
	[[Category: Calcium channel]]		[[Category: Calcium channel]]

OCA at 21:30, 2 October 2014

OCA — Thu, 02 Oct 2014 21:30:50 GMT

←Older revision		Revision as of 21:30, 2 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3bxk\| PDB=3bxk \| SCENE= }}~~	+	==Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex==
-	===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===	+	<StructureSection load='3bxk' size='340' side='right' caption='[[3bxk]], [[Resolution\|resolution]] 2.55Å' scene=''>
-	~~{{ABSTRACT_PUBMED_018400181}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BXK FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
-	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[http://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref><ref>PMID:9345107</ref><ref>PMID:9302278</ref><ref>PMID:16325861</ref><ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[http://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref><ref>PMID:10408532</ref><ref>PMID:11409427</ref><ref>PMID:11439943</ref><ref>PMID:15032980</ref><ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[http://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref><ref>PMID:8898206</ref><ref>PMID:10987655</ref><ref>PMID:11176968</ref><ref>PMID:11723274</ref><ref>PMID:12420090</ref><ref>PMID:15293273</ref><ref>PMID:15173248</ref><ref>PMID:14718690</ref><ref>PMID:18602318</ref><ref>PMID:19232643</ref><ref>PMID:20129625</ref><ref>PMID:21696515</ref>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3bxl\|3bxl]]</td></tr>
-		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
-	==Function==	+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bxk RCSB], [http://www.ebi.ac.uk/pdbsum/3bxk PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[http://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref> <ref>PMID:9345107</ref> <ref>PMID:9302278</ref> <ref>PMID:16325861</ref> <ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[http://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref> <ref>PMID:10408532</ref> <ref>PMID:11409427</ref> <ref>PMID:11439943</ref> <ref>PMID:15032980</ref> <ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[http://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref> <ref>PMID:8898206</ref> <ref>PMID:10987655</ref> <ref>PMID:11176968</ref> <ref>PMID:11723274</ref> <ref>PMID:12420090</ref> <ref>PMID:15293273</ref> <ref>PMID:15173248</ref> <ref>PMID:14718690</ref> <ref>PMID:18602318</ref> <ref>PMID:19232643</ref> <ref>PMID:20129625</ref> <ref>PMID:21696515</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).		[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
-		+	== Evolutionary Conservation ==
-	==~~About this Structure~~==	+	[[Image:Consurf_key_small.gif\|200px\|right]]
-	[[~~3bxk~~]] ~~is a 4 chain~~ structure ~~with sequence from~~ [http://en.~~wikipedia~~.~~org~~/~~wiki/Rattus_norvegicus Rattus norvegicus~~]. ~~Full crystallographic information is~~ available from [http://~~oca~~.~~weizmann~~.ac.il/~~oca-bin~~/~~ocashort~~?id=~~3BXK OCA~~].	+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/3bxk_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>

	==See Also==		==See Also==
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
	*[[MoRFs\|MoRFs]]		*[[MoRFs\|MoRFs]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:018400181</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Kooi, C W.Vander.]]		[[Category: Kooi, C W.Vander.]]

OCA at 01:48, 25 March 2013

OCA — Mon, 25 Mar 2013 01:48:13 GMT

←Older revision		Revision as of 01:48, 25 March 2013
Line 2:		Line 2:
	===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===		===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===
	{{ABSTRACT_PUBMED_018400181}}		{{ABSTRACT_PUBMED_018400181}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_HUMAN]] Defects in CACNA1A are the cause of spinocerebellar ataxia type 6 (SCA6) [MIM:[http://omim.org/entry/183086 183086]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA6 is mainly caused by expansion of a CAG repeat in the coding region of CACNA1A. There seems to be a correlation between the repeat number and earlier onset of the disorder.<ref>PMID:8988170</ref><ref>PMID:9345107</ref><ref>PMID:9302278</ref><ref>PMID:16325861</ref><ref>PMID:20682717</ref> Defects in CACNA1A are the cause of familial hemiplegic migraine type 1 (FHM1) [MIM:[http://omim.org/entry/141500 141500]]; also known as migraine familial hemiplegic 1 (MHP1). FHM1, a rare autosomal dominant subtype of migraine with aura, is associated with ictal hemiparesis and, in some families, progressive cerebellar atrophy.<ref>PMID:8898206</ref><ref>PMID:10408532</ref><ref>PMID:11409427</ref><ref>PMID:11439943</ref><ref>PMID:15032980</ref><ref>PMID:18400034</ref> Defects in CACNA1A are the cause of episodic ataxia type 2 (EA2) [MIM:[http://omim.org/entry/108500 108500]]; also known as acetazolamide-responsive hereditary paroxysmal cerebellar ataxia (APCA). EA2 is an autosomal dominant disorder characterized by acetozolamide-responsive attacks of ataxia, migraine-like symptoms, interictal nystagmus, and cerebellar atrophy.<ref>PMID:9302278</ref><ref>PMID:8898206</ref><ref>PMID:10987655</ref><ref>PMID:11176968</ref><ref>PMID:11723274</ref><ref>PMID:12420090</ref><ref>PMID:15293273</ref><ref>PMID:15173248</ref><ref>PMID:14718690</ref><ref>PMID:18602318</ref><ref>PMID:19232643</ref><ref>PMID:20129625</ref><ref>PMID:21696515</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CAC1A_HUMAN CAC1A_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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).

	==About this Structure==		==About this Structure==
Line 11:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018400181</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018400181</ref><references group="xtra"/><references/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Kooi, C W.Vander.]]		[[Category: Kooi, C W.Vander.]]

OCA at 10:38, 11 March 2013

OCA — Mon, 11 Mar 2013 10:38:03 GMT

←Older revision		Revision as of 10:38, 11 March 2013
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-	[[Image:3bxk.png\|left\|200px]]
-
	{{STRUCTURE_3bxk\| PDB=3bxk \| SCENE= }}		{{STRUCTURE_3bxk\| PDB=3bxk \| SCENE= }}
-
	===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===		===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===
-
	{{ABSTRACT_PUBMED_018400181}}		{{ABSTRACT_PUBMED_018400181}}

Line 12:		Line 8:
	==See Also==		==See Also==
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
		+	*[[MoRFs\|MoRFs]]

	==Reference==		==Reference==

OCA at 12:28, 20 October 2012

OCA — Sat, 20 Oct 2012 12:28:40 GMT

←Older revision		Revision as of 12:28, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3bxk]] is a 4 chain structure ~~of [[Calmodulin]]~~ with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA].	+	[[3bxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA].

	==See Also==		==See Also==

OCA at 08:51, 26 July 2012

OCA — Thu, 26 Jul 2012 08:51:14 GMT

←Older revision		Revision as of 08:51, 26 July 2012
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	[[Image:3bxk.png\|left\|200px]]		[[Image:3bxk.png\|left\|200px]]

-	<!--
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-	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),
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	{{STRUCTURE_3bxk\| PDB=3bxk \| SCENE= }}		{{STRUCTURE_3bxk\| PDB=3bxk \| SCENE= }}

	===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===		===Crystal structure of the P/Q-type calcium channel (CaV2.1) IQ domain and CA2+calmodulin complex===

		+	{{ABSTRACT_PUBMED_018400181}}

	==About this Structure==		==About this Structure==
-	[[3bxk]] is a 4 chain structure of [[Calmodulin~~]] and [[Ion channels~~]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA].	+	[[3bxk]] is a 4 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXK OCA].

	==See Also==		==See Also==
-	*[[Calmodulin]]	+	*[[Calmodulin\|Calmodulin]]
-	*[[Ion channels]]	+
		+	==Reference==
		+	<ref group="xtra">PMID:018400181</ref><references group="xtra"/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Kooi, C W.Vander.]]		[[Category: Kooi, C W.Vander.]]
Line 24:		Line 21:
	[[Category: Yue, D T.]]		[[Category: Yue, D T.]]
	[[Category: Acetylation]]		[[Category: Acetylation]]
-	[[Category: Alternative splicing]]
	[[Category: Calcium channel]]		[[Category: Calcium channel]]
	[[Category: Calcium transport]]		[[Category: Calcium transport]]
Line 45:		Line 41:
	[[Category: Transmembrane]]		[[Category: Transmembrane]]
	[[Category: Transport]]		[[Category: Transport]]
-	[[Category: Ubl conjugation]]
	[[Category: Voltage-gated]]		[[Category: Voltage-gated]]
	[[Category: Voltage-gated channel]]		[[Category: Voltage-gated channel]]