4hex - Revision history

OCA at 08:51, 20 March 2024

2024-03-20T08:51:53Z

← Older revision		Revision as of 08:51, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEX 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=ZN:ZINC+ION'>ZN</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]] 2.001Å</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=ZN:ZINC+ION'>ZN</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [https://pdbe.org/4hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [https://www.ebi.ac.uk/pdbsum/4hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex 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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [https://pdbe.org/4hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [https://www.ebi.ac.uk/pdbsum/4hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] 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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23]		[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] 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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23]
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by approximately 90 degrees at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner.

	A novel trans conformation of ligand-free calmodulin.,Kumar V, Chichili VP, Tang X, Sivaraman J PLoS One. 2013;8(1):e54834. doi: 10.1371/journal.pone.0054834. Epub 2013 Jan 29. PMID:23382982<ref>PMID:23382982</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:13, 3 November 2022

2022-11-03T08:13:19Z

← Older revision		Revision as of 08:13, 3 November 2022
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	==A novel conformation of calmodulin==		==A novel conformation of calmodulin==
	<StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4hex' size='340' side='right'caption='[[4hex]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HEX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEX 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=ZN:ZINC+ION'>ZN</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=ZN:ZINC+ION'>ZN</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])~~</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [https://pdbe.org/4hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [https://www.ebi.ac.uk/pdbsum/4hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex 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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [~~http~~://pdbe.org/4hex PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hex PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] 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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Large Structures]]
	[[Category: ~~Chichili, V P.R~~]]		[[Category: Mus musculus]]
	[[Category: ~~Kumar, V~~]]		[[Category: Chichili VPR]]
	[[Category: ~~Sivaraman, J~~]]		[[Category: Kumar V]]
	[[Category: ~~Calcium binding]]~~		[[Category: Sivaraman J]]
	~~[[Category: Calcium binding protein]]~~
	~~[[Category: Calcium signalling]]~~
	~~[[Category: Calmodulin]]~~
	~~[[Category: Ef-hand motif]]~~
	~~[[Category: Neurogranin]]~~
	~~[[Category: Neuromodulin]]~~
	~~[[Category: Novel conformation]]~~
	~~[[Category: Tran~~]]

OCA at 08:39, 15 November 2017

2017-11-15T08:39:18Z

← Older revision		Revision as of 08:39, 15 November 2017
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Calmodulin\|Calmodulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 01:21, 5 August 2016

2016-08-05T01:21:02Z

← Older revision		Revision as of 01:21, 5 August 2016
Line 1:		Line 1:

	==A novel conformation of calmodulin==		==A novel conformation of calmodulin==
	<StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEX 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=ZN:ZINC+ION'>ZN</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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [http://www.ebi.ac.uk/pdbsum/4hex 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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [http://pdbe.org/4hex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [http://www.ebi.ac.uk/pdbsum/4hex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4hex" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 22:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Chichili, V P.R]]		[[Category: Chichili, V P.R]]
	[[Category: Kumar, V]]		[[Category: Kumar, V]]

OCA at 14:40, 25 December 2014

2014-12-25T14:40:16Z

← Older revision		Revision as of 14:40, 25 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4hex~~.~~jpg~~\|~~left~~\|~~200px~~]]		==A novel conformation of calmodulin==
			<StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEX 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=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [http://www.ebi.ac.uk/pdbsum/4hex PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by approximately 90 degrees at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner.

	~~{{STRUCTURE_4hex\| PDB=4hex \| SCENE= }}~~		A novel trans conformation of ligand-free calmodulin.,Kumar V, Chichili VP, Tang X, Sivaraman J PLoS One. 2013;8(1):e54834. doi: 10.1371/journal.pone.0054834. Epub 2013 Jan 29. PMID:23382982<ref>PMID:23382982</ref>

	~~===A novel conformation~~ of ~~calmodulin===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_23382982}}~~		==See Also==
			*[[Calmodulin\|Calmodulin]]
	==~~About this Structure~~==		== References ==
	[[~~4hex~~]] ~~is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Chichili, V P.R.]]		[[Category: Chichili, V P.R]]
	[[Category: Kumar, V.]]		[[Category: Kumar, V]]
	[[Category: Sivaraman, J.]]		[[Category: Sivaraman, J]]
	[[Category: Calcium binding]]		[[Category: Calcium binding]]
	[[Category: Calcium binding protein]]		[[Category: Calcium binding protein]]

OCA at 14:12, 6 March 2013

2013-03-06T14:12:42Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4hex.jpg|left|200px]]
-The entry 4hex is ON HOLD  until Paper Publication
+{{STRUCTURE_4hex|  PDB=4hex  |  SCENE=  }}
-Authors: Kumar, V., Chichili, V.P.R., Sivaraman, J.
+===A novel conformation of calmodulin===
-Description: A novel conformation of calmodulin
+{{ABSTRACT_PUBMED_23382982}}

OCA at 10:59, 19 December 2012

2012-12-19T10:59:06Z

← Older revision		Revision as of 10:59, 19 December 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4hex is ON HOLD		The entry 4hex is ON HOLD until Paper Publication

	Authors: Kumar, V., Chichili, V.P.R., Sivaraman, J.		Authors: Kumar, V., Chichili, V.P.R., Sivaraman, J.

	Description: A novel conformation of calmodulin		Description: A novel conformation of calmodulin

OCA at 08:38, 31 October 2012

2012-10-31T08:38:14Z

← Older revision		Revision as of 08:38, 31 October 2012
Line 3:		Line 3:
	The entry 4hex is ON HOLD		The entry 4hex is ON HOLD

	Authors: ~~Veerendra~~ Kumar, ~~Vishnu Priyanka Reddy~~ Chichili, J ~~Sivaraman~~		Authors: Kumar, V., Chichili, V.P.R., Sivaraman, J.

	Description: A novel conformation of calmodulin		Description: A novel conformation of calmodulin

OCA: Protected "4hex" [edit=sysop:move=sysop]

2012-10-10T07:02:04Z

Protected "4hex" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:02, 10 October 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4hex is ON HOLD Authors: Veerendra Kumar, Vishnu Priyanka Reddy Chichili, J Sivaraman Description: A novel conformation of calmodulin

2012-10-10T07:02:03Z

New page: '''Unreleased structure''' The entry 4hex is ON HOLD Authors: Veerendra Kumar, Vishnu Priyanka Reddy Chichili, J Sivaraman Description: A novel conformation of calmodulin

New page

'''Unreleased structure'''

The entry 4hex is ON HOLD

Authors: Veerendra Kumar, Vishnu Priyanka Reddy Chichili, J Sivaraman

Description: A novel conformation of calmodulin