1a2x - Revision history

OCA at 06:27, 7 February 2024

2024-02-07T06:27:04Z

←Older revision		Revision as of 06:27, 7 February 2024
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	<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~European_rabbit European rabbit~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2X FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [https://pdbe.org/1a2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [https://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [https://pdbe.org/1a2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [https://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. [[https://www.uniprot.org/uniprot/TNNI2_RABIT TNNI2_RABIT]] Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.	+	[https://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1a2x 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=1a2x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Troponin (Tn), the complex of three subunits (TnC, TnI, and TnT), plays a key role in Ca2+-dependent regulation of muscle contraction. To elucidate the interactions between the Tn subunits and the conformation of TnC in the Tn complex, we have determined the crystal structure of TnC (two Ca2+ bound state) in complex with the N-terminal fragment of TnI (TnI1-47). The structure was solved by the single isomorphous replacement method in combination with multiple wavelength anomalous dispersion data. The refinement converged to a crystallographic R factor of 22.2% (Rfree = 32.6%). The central, connecting alpha-helix observed in the structure of uncomplexed TnC (TnCfree) is unwound at the center (residues Ala-87, Lys-88, Gly-89, Lys-90, and Ser-91) and bent by 90 degrees. As a result, TnC in the complex has a compact globular shape with direct interactions between the N- and C-terminal lobes, in contrast to the elongated dumb-bell shaped molecule of uncomplexed TnC. The 31-residue long TnI1-47 alpha-helix stretches on the surface of TnC and stabilizes its compact conformation by multiple contacts with both TnC lobes. The amphiphilic C-end of the TnI1-47 alpha-helix is bound in the hydrophobic pocket of the TnC C-lobe through 38 van der Waals interactions. The results indicate the major difference between Ca2+ receptors integrated with the other proteins (TnC in Tn) and isolated in the cytosol (calmodulin). The TnC/TnI1-47 structure implies a mechanism of how Tn regulates the muscle contraction and suggests a unique alpha-helical regulatory TnI segment, which binds to the N-lobe of TnC in its Ca2+ bound conformation.
-
-	Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution.,Vassylyev DG, Takeda S, Wakatsuki S, Maeda K, Maeda Y Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4847-52. PMID:9560191<ref>PMID:9560191</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1a2x" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Troponin\|Troponin]]	+	*[[Troponin 3D structures\|Troponin 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: European rabbit]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Maeda, K]]	+	[[Category: Oryctolagus cuniculus]]
-	[[Category: Maeda, Y]]	+	[[Category: Maeda K]]
-	[[Category: Takeda, S]]	+	[[Category: Maeda Y]]
-	[[Category: Vassylyev~~, D G~~]]	+	[[Category: Takeda S]]
-	[[Category: Wakatsuki, S]]	+	[[Category: Vassylyev DG]]
-	~~[[Category: Muscle contraction regulation]]~~	+	[[Category: Wakatsuki S]]
-	~~[[Category: Troponin~~]]	+

OCA at 09:41, 26 May 2021

2021-05-26T09:41:42Z

←Older revision		Revision as of 09:41, 26 May 2021
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	<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1A2X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2X 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='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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [~~http~~://pdbe.org/1a2x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [https://pdbe.org/1a2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [https://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. [[~~http~~://www.uniprot.org/uniprot/TNNI2_RABIT TNNI2_RABIT]] Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.	+	[[https://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. [[https://www.uniprot.org/uniprot/TNNI2_RABIT TNNI2_RABIT]] Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]
	*[[Troponin\|Troponin]]		*[[Troponin\|Troponin]]
	== References ==		== References ==

OCA at 07:51, 21 August 2019

2019-08-21T07:51:43Z

←Older revision		Revision as of 07:51, 21 August 2019
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	==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==		==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==
-	<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X 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/a2/1a2x_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a2/1a2x_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 31:		Line 31:
	==See Also==		==See Also==
	*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]		*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]
		+	*[[Troponin\|Troponin]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: European rabbit]]		[[Category: European rabbit]]
		+	[[Category: Large Structures]]
	[[Category: Maeda, K]]		[[Category: Maeda, K]]
	[[Category: Maeda, Y]]		[[Category: Maeda, Y]]

OCA at 10:49, 15 November 2017

2017-11-15T10:49:23Z

←Older revision		Revision as of 10:49, 15 November 2017
Line 1:		Line 1:
		+
	==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==		==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==
	<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X 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='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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://pdbe.org/1a2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://pdbe.org/1a2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 31:
	==See Also==		==See Also==
	*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]		*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]
-	*[[Troponin\|Troponin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:43, 9 February 2016

2016-02-09T19:43:05Z

←Older revision		Revision as of 19:43, 9 February 2016
Line 16:		Line 16:
	<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=1a2x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 16:07, 9 September 2015

2015-09-09T16:07:24Z

←Older revision		Revision as of 16:07, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Oryctolagus_cuniculus Oryctolagus cuniculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X 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='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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://pdbe.org/1a2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		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 1a2x" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Oryctolagus cuniculus~~]]	+	[[Category: European rabbit]]
	[[Category: Maeda, K]]		[[Category: Maeda, K]]
	[[Category: Maeda, Y]]		[[Category: Maeda, Y]]

OCA at 09:07, 25 December 2014

2014-12-25T09:07:06Z

←Older revision		Revision as of 09:07, 25 December 2014
Line 6:		Line 6:
	<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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. [[http://www.uniprot.org/uniprot/TNNI2_RABIT TNNI2_RABIT]] Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:11, 22 December 2014

2014-12-22T12:11:20Z

←Older revision		Revision as of 12:11, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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></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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	[[Category: Maeda, K.]]	+	[[Category: Maeda, K]]
-	[[Category: Maeda, Y.]]	+	[[Category: Maeda, Y]]
-	[[Category: Takeda, S.]]	+	[[Category: Takeda, S]]
-	[[Category: Vassylyev, D G.]]	+	[[Category: Vassylyev, D G]]
-	[[Category: Wakatsuki, S.]]	+	[[Category: Wakatsuki, S]]
	[[Category: Muscle contraction regulation]]		[[Category: Muscle contraction regulation]]
	[[Category: Troponin]]		[[Category: Troponin]]

OCA at 08:38, 23 July 2014

2014-07-23T08:38:16Z

←Older revision		Revision as of 08:38, 23 July 2014
Line 1:		Line 1:
-	[[~~Image~~:1a2x.~~png\|left~~\|200px]]	+	==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==
		+	<StructureSection load='1a2x' size='340' side='right' caption='[[1a2x]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A2X FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [http://www.ebi.ac.uk/pdbsum/1a2x 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/a2/1a2x_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 ==
		+	Troponin (Tn), the complex of three subunits (TnC, TnI, and TnT), plays a key role in Ca2+-dependent regulation of muscle contraction. To elucidate the interactions between the Tn subunits and the conformation of TnC in the Tn complex, we have determined the crystal structure of TnC (two Ca2+ bound state) in complex with the N-terminal fragment of TnI (TnI1-47). The structure was solved by the single isomorphous replacement method in combination with multiple wavelength anomalous dispersion data. The refinement converged to a crystallographic R factor of 22.2% (Rfree = 32.6%). The central, connecting alpha-helix observed in the structure of uncomplexed TnC (TnCfree) is unwound at the center (residues Ala-87, Lys-88, Gly-89, Lys-90, and Ser-91) and bent by 90 degrees. As a result, TnC in the complex has a compact globular shape with direct interactions between the N- and C-terminal lobes, in contrast to the elongated dumb-bell shaped molecule of uncomplexed TnC. The 31-residue long TnI1-47 alpha-helix stretches on the surface of TnC and stabilizes its compact conformation by multiple contacts with both TnC lobes. The amphiphilic C-end of the TnI1-47 alpha-helix is bound in the hydrophobic pocket of the TnC C-lobe through 38 van der Waals interactions. The results indicate the major difference between Ca2+ receptors integrated with the other proteins (TnC in Tn) and isolated in the cytosol (calmodulin). The TnC/TnI1-47 structure implies a mechanism of how Tn regulates the muscle contraction and suggests a unique alpha-helical regulatory TnI segment, which binds to the N-lobe of TnC in its Ca2+ bound conformation.

-	~~{{STRUCTURE_1a2x\| PDB=1a2x \| SCENE= }}~~	+	Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution.,Vassylyev DG, Takeda S, Wakatsuki S, Maeda K, Maeda Y Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4847-52. PMID:9560191<ref>PMID:9560191</ref>

-	~~===COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9560191}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1a2x]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA].~~	+

	==See Also==		==See Also==
		+	*[[Role of Troponin C in decreased muscle sensitivity to calcium\|Role of Troponin C in decreased muscle sensitivity to calcium]]
	*[[Troponin\|Troponin]]		*[[Troponin\|Troponin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009560191<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Maeda, K.]]		[[Category: Maeda, K.]]

OCA at 14:55, 20 October 2012

2012-10-20T14:55:35Z

←Older revision		Revision as of 14:55, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1a2x]] is a 2 chain structure ~~of [[Troponin]]~~ with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA].	+	[[1a2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA].

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