1mux - Revision history

OCA at 08:51, 22 May 2024

2024-05-22T08:51:10Z

←Older revision		Revision as of 08:51, 22 May 2024
Line 20:		Line 20:
	</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=1mux 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=1mux ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition.
		+
		+	Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.,Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M J Mol Biol. 1998 Feb 13;276(1):165-76. PMID:9514729<ref>PMID:9514729</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1mux" 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 08:42, 10 April 2024

2024-04-10T08:42:10Z

←Older revision		Revision as of 08:42, 10 April 2024
Line 1:		Line 1:

	==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==		==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==
-	<StructureSection load='1mux' size='340' side='right'caption='[[1mux~~]], [[NMR_Ensembles_of_Models \| 30 NMR models~~]]' scene=''>	+	<StructureSection load='1mux' size='340' side='right'caption='[[1mux]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~African_clawed_frog African clawed frog~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [https://pdbe.org/1mux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [https://www.ebi.ac.uk/pdbsum/1mux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux 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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [https://pdbe.org/1mux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [https://www.ebi.ac.uk/pdbsum/1mux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~CALM_XENLA CALM_XENLA]~~] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.	+	[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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=1mux 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=1mux ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition.
-
-	Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.,Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M J Mol Biol. 1998 Feb 13;276(1):165-76. PMID:9514729<ref>PMID:9514729</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1mux" 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>
-	[[Category: African clawed frog]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Furuya, T]]	+	[[Category: Xenopus laevis]]
-	[[Category: Ikura, M]]	+	[[Category: Furuya T]]
-	[[Category: Mase, T]]	+	[[Category: Ikura M]]
-	[[Category: Osawa, M]]	+	[[Category: Mase T]]
-	[[Category: Swindells~~, M B~~]]	+	[[Category: Osawa M]]
-	[[Category: Tanaka, T]]	+	[[Category: Swindells MB]]
-	[[Category: Tanikawa, J]]	+	[[Category: Tanaka T]]
-	~~[[Category: Calcium-binding]]~~	+	[[Category: Tanikawa J]]
-	~~[[Category: Calmodulin]]~~	+
-	~~[[Category: Naphthalenesulfonamide]]~~	+
-	~~[[Category: W-7~~]]	+

OCA at 09:29, 5 May 2021

2021-05-05T09:29:56Z

←Older revision		Revision as of 09:29, 5 May 2021
Line 3:		Line 3:
	<StructureSection load='1mux' size='340' side='right'caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1mux' size='340' side='right'caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MUX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene></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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [~~http~~://pdbe.org/1mux PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1mux PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux 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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [https://pdbe.org/1mux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [https://www.ebi.ac.uk/pdbsum/1mux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.	+	[[https://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:37, 31 July 2019

2019-07-31T07:37:35Z

←Older revision		Revision as of 07:37, 31 July 2019
Line 1:		Line 1:

	==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==		==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==
-	<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>	+	<StructureSection load='1mux' size='340' side='right'caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mux_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mux_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>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: African clawed frog]]		[[Category: African clawed frog]]
		+	[[Category: Large Structures]]
	[[Category: Furuya, T]]		[[Category: Furuya, T]]
	[[Category: Ikura, M]]		[[Category: Ikura, M]]

OCA at 10:24, 25 October 2017

2017-10-25T10:24:45Z

←Older revision		Revision as of 10:24, 25 October 2017
Line 1:		Line 1:
		+
	==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==		==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==
	<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene></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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://pdbe.org/1mux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux 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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://pdbe.org/1mux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	<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=1mux ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Calmodulin\|Calmodulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:19, 12 September 2015

2015-09-12T02:19:51Z

←Older revision		Revision as of 02:19, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Xenopus_laevis Xenopus laevis~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene></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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux 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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://pdbe.org/1mux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	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 1mux" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 31:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Xenopus laevis~~]]	+	[[Category: African clawed frog]]
	[[Category: Furuya, T]]		[[Category: Furuya, T]]
	[[Category: Ikura, M]]		[[Category: Ikura, M]]

OCA at 16:42, 5 January 2015

2015-01-05T16:42:26Z

←Older revision		Revision as of 16:42, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene></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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux 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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]
-	[[Category: Furuya, T.]]	+	[[Category: Furuya, T]]
-	[[Category: Ikura, M.]]	+	[[Category: Ikura, M]]
-	[[Category: Mase, T.]]	+	[[Category: Mase, T]]
-	[[Category: Osawa, M.]]	+	[[Category: Osawa, M]]
-	[[Category: Swindells, M B.]]	+	[[Category: Swindells, M B]]
-	[[Category: Tanaka, T.]]	+	[[Category: Tanaka, T]]
-	[[Category: Tanikawa, J.]]	+	[[Category: Tanikawa, J]]
	[[Category: Calcium-binding]]		[[Category: Calcium-binding]]
	[[Category: Calmodulin]]		[[Category: Calmodulin]]
	[[Category: Naphthalenesulfonamide]]		[[Category: Naphthalenesulfonamide]]
	[[Category: W-7]]		[[Category: W-7]]

OCA at 18:05, 28 September 2014

2014-09-28T18:05:49Z

←Older revision		Revision as of 18:05, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1mux.~~png\|left~~\|200px]]	+	==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==
		+	<StructureSection load='1mux' size='340' side='right' caption='[[1mux]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUX 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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene><br>
		+	<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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [http://www.ebi.ac.uk/pdbsum/1mux PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mux_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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition.

-	~~{{STRUCTURE_1mux\| PDB=1mux \| SCENE= }}~~	+	Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.,Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M J Mol Biol. 1998 Feb 13;276(1):165-76. PMID:9514729<ref>PMID:9514729</ref>

-	~~===SOLUTION NMR STRUCTURE OF CALMODULIN~~/~~W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION~~, ~~30 STRUCTURES===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9514729}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1mux]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Xenopus_laevis Xenopus laevis]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA].~~	+

	==See Also==		==See Also==
	*[[Calmodulin\|Calmodulin]]		*[[Calmodulin\|Calmodulin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009514729<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]
	[[Category: Furuya, T.]]		[[Category: Furuya, T.]]

OCA at 22:27, 20 October 2012

2012-10-20T22:27:55Z

←Older revision		Revision as of 22:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1mux]] is a 1 chain structure ~~of [[Calmodulin]]~~ with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA].	+	[[1mux]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA].

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

OCA: Protected "1mux" [edit=sysop:move=sysop]

2012-07-27T16:23:24Z

Protected "1mux" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:23, 27 July 2012