1tnw - Revision history

OCA at 09:13, 22 May 2024

2024-05-22T09:13:12Z

←Older revision		Revision as of 09:13, 22 May 2024
Line 19:		Line 19:
	</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=1tnw 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=1tnw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution structure of TnC which has been solved using 3D and 4D heteronuclear nuclear magnetic resonance (NMR) spectroscopic techniques. The 1H, 13C, and 15N backbone chemical shifts have already been published [Slupsky, C. M., Reinach, F. C., Smillie, L. B., & Sykes, B. D. (1995) Protein Sci. 4, 1279-1290]. Presented herein are the 1H, 13C, and 15N side-chain chemical shifts which are 80% complete. The structure of calcium-saturated TnC was determined on the basis of 2106 NOE-derived distance restraints, 121 phi dihedral angle restraints, and 76 psi dihedral angle restraints. The appearance of calcium-saturated TnC reveals a dumbbell-shaped molecule with two globular domains connected by a linker. The structures of the N-terminal and C-terminal domains are highly converged [backbone atomic root mean square deviations (rmsd) about the mean atomic coordinate position for residues 10-80 and 98-155 are 0.66 +/- 0.17 and 0.69 +/- 0.18 A, respectively]; however, the orientation of one domain with respect to the other is not well-defined, and thus each domain appears to be structurally independent. Comparison of the calcium-saturated form of TnC determined herein with the half-saturated form determined by X-ray methods reveals two major differences. First, there is a major structural change which occurs in the N-terminal domain resulting in the opening of a hydrophobic pocket presumably to present itself to its target protein troponin I. This structural change appears to involve only helices B and C which move away from helices N/A/D by the alteration of the backbone phi, psi angles of glutamic acid 41 from irregular in the crystal structure (-97 degrees, -7 degrees) to helical in the NMR calcium-saturated structure (-60 degrees, -34 degrees). The other difference between the two structures is the presence of a flexible linker between the two domains in the NMR structure. This flexible linker allows the two domains of TnC to adopt any orientation with respect to one another such that they can interact with a variety of targets.
		+
		+	NMR solution structure of calcium-saturated skeletal muscle troponin C.,Slupsky CM, Sykes BD Biochemistry. 1995 Dec 12;34(49):15953-64. PMID:8519752<ref>PMID:8519752</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1tnw" style="background-color:#fffaf0;"></div>

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

OCA at 08:42, 1 May 2024

2024-05-01T08:42:50Z

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

	==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==		==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==
-	<StructureSection load='1tnw' size='340' side='right'caption='[[1tnw~~]], [[NMR_Ensembles_of_Models \| 23 NMR models~~]]' scene=''>	+	<StructureSection load='1tnw' size='340' side='right'caption='[[1tnw]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Chick Chick~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TNW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1tnx\|1tnx]]</div~~></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [https://pdbe.org/1tnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [https://www.ebi.ac.uk/pdbsum/1tnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnw 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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [https://pdbe.org/1tnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [https://www.ebi.ac.uk/pdbsum/1tnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] 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/TNNC2_CHICK TNNC2_CHICK] 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]]
Line 19:		Line 19:
	</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=1tnw 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=1tnw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution structure of TnC which has been solved using 3D and 4D heteronuclear nuclear magnetic resonance (NMR) spectroscopic techniques. The 1H, 13C, and 15N backbone chemical shifts have already been published [Slupsky, C. M., Reinach, F. C., Smillie, L. B., & Sykes, B. D. (1995) Protein Sci. 4, 1279-1290]. Presented herein are the 1H, 13C, and 15N side-chain chemical shifts which are 80% complete. The structure of calcium-saturated TnC was determined on the basis of 2106 NOE-derived distance restraints, 121 phi dihedral angle restraints, and 76 psi dihedral angle restraints. The appearance of calcium-saturated TnC reveals a dumbbell-shaped molecule with two globular domains connected by a linker. The structures of the N-terminal and C-terminal domains are highly converged [backbone atomic root mean square deviations (rmsd) about the mean atomic coordinate position for residues 10-80 and 98-155 are 0.66 +/- 0.17 and 0.69 +/- 0.18 A, respectively]; however, the orientation of one domain with respect to the other is not well-defined, and thus each domain appears to be structurally independent. Comparison of the calcium-saturated form of TnC determined herein with the half-saturated form determined by X-ray methods reveals two major differences. First, there is a major structural change which occurs in the N-terminal domain resulting in the opening of a hydrophobic pocket presumably to present itself to its target protein troponin I. This structural change appears to involve only helices B and C which move away from helices N/A/D by the alteration of the backbone phi, psi angles of glutamic acid 41 from irregular in the crystal structure (-97 degrees, -7 degrees) to helical in the NMR calcium-saturated structure (-60 degrees, -34 degrees). The other difference between the two structures is the presence of a flexible linker between the two domains in the NMR structure. This flexible linker allows the two domains of TnC to adopt any orientation with respect to one another such that they can interact with a variety of targets.
-
-	NMR solution structure of calcium-saturated skeletal muscle troponin C.,Slupsky CM, Sykes BD Biochemistry. 1995 Dec 12;34(49):15953-64. PMID:8519752<ref>PMID:8519752</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1tnw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Troponin\|Troponin]]	+	*[[Troponin 3D structures\|Troponin 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chick~~]]	+	[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Slupsky~~, C M~~]]	+	[[Category: Slupsky CM]]
-	[[Category: Sykes~~, B D]]~~	+	[[Category: Sykes BD]]
-	~~[[Category: Calcium-binding protein]]~~	+
-	~~[[Category: Ef-hand~~]]	+

OCA at 09:30, 29 September 2021

2021-09-29T09:30:14Z

←Older revision		Revision as of 09:30, 29 September 2021
Line 3:		Line 3:
	<StructureSection load='1tnw' size='340' side='right'caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='1tnw' size='340' side='right'caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1TNW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tnx\|1tnx]]</div></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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [~~http~~://pdbe.org/1tnw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1tnw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnw 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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [https://pdbe.org/1tnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [https://www.ebi.ac.uk/pdbsum/1tnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] 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/TNNC2_CHICK TNNC2_CHICK]] 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]]

OCA at 14:08, 25 December 2019

2019-12-25T14:08:04Z

←Older revision		Revision as of 14:08, 25 December 2019
Line 1:		Line 1:

	==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==		==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==
-	<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>	+	<StructureSection load='1tnw' size='340' side='right'caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Chick]]		[[Category: Chick]]
		+	[[Category: Large Structures]]
	[[Category: Slupsky, C M]]		[[Category: Slupsky, C M]]
	[[Category: Sykes, B D]]		[[Category: Sykes, B D]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Ef-hand]]		[[Category: Ef-hand]]

OCA at 08:57, 21 March 2018

2018-03-21T08:57:37Z

←Older revision		Revision as of 08:57, 21 March 2018
Line 1:		Line 1:
		+
	==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==		==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==
	<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://pdbe.org/1tnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw 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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://pdbe.org/1tnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tn/1tnw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tn/1tnw_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 05:05, 9 February 2016

2016-02-09T05:05:20Z

←Older revision		Revision as of 05:05, 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=1tnw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 18:54, 10 September 2015

2015-09-10T18:54:45Z

←Older revision		Revision as of 18:54, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Gallus_gallus Gallus gallus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw 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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://pdbe.org/1tnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw 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 1tnw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gallus gallus~~]]	+	[[Category: Chick]]
	[[Category: Slupsky, C M]]		[[Category: Slupsky, C M]]
	[[Category: Sykes, B D]]		[[Category: Sykes, B D]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Ef-hand]]		[[Category: Ef-hand]]

OCA at 04:37, 25 December 2014

2014-12-25T04:37:31Z

←Older revision		Revision as of 04:37, 25 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw 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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] 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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	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
-	[[Category: Slupsky, C M.]]	+	[[Category: Slupsky, C M]]
-	[[Category: Sykes, B D.]]	+	[[Category: Sykes, B D]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Ef-hand]]		[[Category: Ef-hand]]

OCA at 22:03, 28 September 2014

2014-09-28T22:03:19Z

←Older revision		Revision as of 22:03, 28 September 2014
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-	[[~~Image:~~1tnw.~~png~~\|~~left~~\|200px]]	+	==NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C==
		+	<StructureSection load='1tnw' size='340' side='right' caption='[[1tnw]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TNW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tnx\|1tnx]]</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=1tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tnw RCSB], [http://www.ebi.ac.uk/pdbsum/1tnw 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/tn/1tnw_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 C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution structure of TnC which has been solved using 3D and 4D heteronuclear nuclear magnetic resonance (NMR) spectroscopic techniques. The 1H, 13C, and 15N backbone chemical shifts have already been published [Slupsky, C. M., Reinach, F. C., Smillie, L. B., & Sykes, B. D. (1995) Protein Sci. 4, 1279-1290]. Presented herein are the 1H, 13C, and 15N side-chain chemical shifts which are 80% complete. The structure of calcium-saturated TnC was determined on the basis of 2106 NOE-derived distance restraints, 121 phi dihedral angle restraints, and 76 psi dihedral angle restraints. The appearance of calcium-saturated TnC reveals a dumbbell-shaped molecule with two globular domains connected by a linker. The structures of the N-terminal and C-terminal domains are highly converged [backbone atomic root mean square deviations (rmsd) about the mean atomic coordinate position for residues 10-80 and 98-155 are 0.66 +/- 0.17 and 0.69 +/- 0.18 A, respectively]; however, the orientation of one domain with respect to the other is not well-defined, and thus each domain appears to be structurally independent. Comparison of the calcium-saturated form of TnC determined herein with the half-saturated form determined by X-ray methods reveals two major differences. First, there is a major structural change which occurs in the N-terminal domain resulting in the opening of a hydrophobic pocket presumably to present itself to its target protein troponin I. This structural change appears to involve only helices B and C which move away from helices N/A/D by the alteration of the backbone phi, psi angles of glutamic acid 41 from irregular in the crystal structure (-97 degrees, -7 degrees) to helical in the NMR calcium-saturated structure (-60 degrees, -34 degrees). The other difference between the two structures is the presence of a flexible linker between the two domains in the NMR structure. This flexible linker allows the two domains of TnC to adopt any orientation with respect to one another such that they can interact with a variety of targets.

-	~~{{STRUCTURE_1tnw\| PDB=1tnw \| SCENE= }}~~	+	NMR solution structure of calcium-saturated skeletal muscle troponin C.,Slupsky CM, Sykes BD Biochemistry. 1995 Dec 12;34(49):15953-64. PMID:8519752<ref>PMID:8519752</ref>

-	~~===NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8519752}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1tnw]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Gallus_gallus Gallus gallus]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA].~~	+

	==See Also==		==See Also==
	*[[Troponin\|Troponin]]		*[[Troponin\|Troponin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008519752<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Slupsky, C M.]]		[[Category: Slupsky, C M.]]

OCA at 12:44, 20 October 2012

2012-10-20T12:44:29Z

←Older revision		Revision as of 12:44, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1tnw]] is a 1 chain structure ~~of [[Troponin]]~~ with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA].	+	[[1tnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNW OCA].

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