6e2f - Revision history

OCA at 14:38, 13 March 2024

2024-03-13T14:38:49Z

←Older revision		Revision as of 14:38, 13 March 2024
Line 3:		Line 3:
	<SX load='6e2f' size='340' side='right' viewer='molstar' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>		<SX load='6e2f' size='340' side='right' viewer='molstar' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6E2F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E2F 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">Electron Microscopy, [[Resolution\|Resolution]] 3.9Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~TRPV6, ECAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN]), CALM1, CALM, CAM, CAM1 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [~~http~~://pdbe.org/6e2f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f 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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [https://pdbe.org/6e2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [https://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[http://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 ==
-	[~~[http~~://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN]] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</ref> [[http://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>	+	[https://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Calcium (Ca(2+)) plays a major role in numerous physiological processes. Ca(2+) homeostasis is tightly controlled by ion channels, the aberrant regulation of which results in various diseases including cancers. Calmodulin (CaM)-mediated Ca(2+)-induced inactivation is an ion channel regulatory mechanism that protects cells against the toxic effects of Ca(2+) overload. We used cryo-electron microscopy to capture the epithelial calcium channel TRPV6 (transient receptor potential vanilloid subfamily member 6) inactivated by CaM. The TRPV6-CaM complex exhibits 1:1 stoichiometry; one TRPV6 tetramer binds both CaM lobes, which adopt a distinct head-to-tail arrangement. The CaM carboxyl-terminal lobe plugs the channel through a unique cation-pi interaction by inserting the side chain of lysine K115 into a tetra-tryptophan cage at the pore's intracellular entrance. We propose a mechanism of CaM-mediated Ca(2+)-induced inactivation that can be explored for therapeutic design.	+
-		+
-	Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6.,Singh AK, McGoldrick LL, Twomey EC, Sobolevsky AI Sci Adv. 2018 Aug 15;4(8):eaau6088. doi: 10.1126/sciadv.aau6088. eCollection 2018, Aug. PMID:30116787<ref>PMID:30116787</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6e2f" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
		+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: McGoldrick~~, L L~~]]	+	[[Category: McGoldrick LL]]
-	[[Category: Singh~~, A K~~]]	+	[[Category: Singh AK]]
-	[[Category: Sobolevsky~~, A I]]~~	+	[[Category: Sobolevsky AI]]
-	~~[[Category: Calcium channel]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Trp channel]]~~	+
-	~~[[Category: Trpv6~~]]	+

OCA at 00:18, 11 April 2020

2020-04-11T00:18:27Z

←Older revision		Revision as of 00:18, 11 April 2020
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	<SX load='6e2f' size='340' side='right' viewer='molstar' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>		<SX load='6e2f' size='340' side='right' viewer='molstar' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6E2F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E2F 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">TRPV6, ECAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALM1, CALM, CAM, CAM1 ([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">TRPV6, ECAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALM1, CALM, CAM, CAM1 ([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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 21:00, 6 March 2020

2020-03-06T21:00:32Z

←Older revision		Revision as of 21:00, 6 March 2020
Line 1:		Line 1:

	==Cryo-EM structure of human TRPV6 in complex with Calmodulin==		==Cryo-EM structure of human TRPV6 in complex with Calmodulin==
-	<~~StructureSection~~ load='6e2f' size='340' side='right'caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>	+	<SX load='6e2f' size='340' side='right' viewer='molstar' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>		<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>
Line 27:		Line 27:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 10:23, 18 December 2019

2019-12-18T10:23:13Z

←Older revision		Revision as of 10:23, 18 December 2019
Line 1:		Line 1:

	==Cryo-EM structure of human TRPV6 in complex with Calmodulin==		==Cryo-EM structure of human TRPV6 in complex with Calmodulin==
-	<StructureSection load='6e2f' size='340' side='right' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>	+	<StructureSection load='6e2f' size='340' side='right'caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>		<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 6e2f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6e2f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: McGoldrick, L L]]		[[Category: McGoldrick, L L]]
	[[Category: Singh, A K]]		[[Category: Singh, A K]]

OCA at 06:51, 24 October 2018

2018-10-24T06:51:15Z

←Older revision		Revision as of 06:51, 24 October 2018
Line 3:		Line 3:
	<StructureSection load='6e2f' size='340' side='right' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>		<StructureSection load='6e2f' size='340' side='right' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6e2f]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6e2f]] is a 5 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=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F 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">TRPV6, ECAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CALM1, CALM, CAM, CAM1 ([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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f 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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN]] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</ref> [[http://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>		[[http://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN]] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</ref> [[http://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;">
		+	== Publication Abstract from PubMed ==
		+	Calcium (Ca(2+)) plays a major role in numerous physiological processes. Ca(2+) homeostasis is tightly controlled by ion channels, the aberrant regulation of which results in various diseases including cancers. Calmodulin (CaM)-mediated Ca(2+)-induced inactivation is an ion channel regulatory mechanism that protects cells against the toxic effects of Ca(2+) overload. We used cryo-electron microscopy to capture the epithelial calcium channel TRPV6 (transient receptor potential vanilloid subfamily member 6) inactivated by CaM. The TRPV6-CaM complex exhibits 1:1 stoichiometry; one TRPV6 tetramer binds both CaM lobes, which adopt a distinct head-to-tail arrangement. The CaM carboxyl-terminal lobe plugs the channel through a unique cation-pi interaction by inserting the side chain of lysine K115 into a tetra-tryptophan cage at the pore's intracellular entrance. We propose a mechanism of CaM-mediated Ca(2+)-induced inactivation that can be explored for therapeutic design.
		+
		+	Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6.,Singh AK, McGoldrick LL, Twomey EC, Sobolevsky AI Sci Adv. 2018 Aug 15;4(8):eaau6088. doi: 10.1126/sciadv.aau6088. eCollection 2018, Aug. PMID:30116787<ref>PMID:30116787</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6e2f" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: McGoldrick, L L]]		[[Category: McGoldrick, L L]]
	[[Category: Singh, A K]]		[[Category: Singh, A K]]

OCA at 06:09, 22 August 2018

2018-08-22T06:09:10Z

←Older revision		Revision as of 06:09, 22 August 2018
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-	'''Unreleased structure'''

-	The entry ~~6e2f~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Cryo-EM structure of human TRPV6 in complex with Calmodulin==
-		+	<StructureSection load='6e2f' size='340' side='right' caption='[[6e2f]], [[Resolution\|resolution]] 3.90Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6e2f]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br>
-	~~Description~~:	+	</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>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://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 ==
		+	[[http://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN]] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</ref> [[http://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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: McGoldrick, L L]]
		+	[[Category: Singh, A K]]
		+	[[Category: Sobolevsky, A I]]
		+	[[Category: Calcium channel]]
		+	[[Category: Membrane protein]]
		+	[[Category: Trp channel]]
		+	[[Category: Trpv6]]

OCA at 17:01, 1 August 2018

2018-08-01T17:01:37Z

←Older revision		Revision as of 17:01, 1 August 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6e2f is ON HOLD	+	The entry 6e2f is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6e2f" [edit=sysop:move=sysop]

2018-07-18T05:42:34Z

Protected "6e2f" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:42, 18 July 2018

OCA: New page: '''Unreleased structure''' The entry 6e2f is ON HOLD Authors: Description: Category: Unreleased Structures

2018-07-18T05:42:33Z

New page: '''Unreleased structure''' The entry 6e2f is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6e2f is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]