1pon - Revision history

OCA at 05:57, 17 April 2024

OCA — Wed, 17 Apr 2024 05:57:30 GMT

←Older revision		Revision as of 05:57, 17 April 2024
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	==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==		==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==
-	<StructureSection load='1pon' size='340' side='right'caption='[[1pon~~]], [[NMR_Ensembles_of_Models \| 42 NMR models~~]]' scene=''>	+	<StructureSection load='1pon' size='340' side='right'caption='[[1pon]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PON FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PON FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [https://pdbe.org/1pon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [https://www.ebi.ac.uk/pdbsum/1pon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pon 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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [https://pdbe.org/1pon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [https://www.ebi.ac.uk/pdbsum/1pon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pon 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 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=1pon 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=1pon ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The C-terminal domain from the muscle protein troponin C (TnC) comprises two helix-loop-helix calcium-binding sites (residues 90-162). The assembly of these two sites is governed by calcium binding enabling a synthetic C-terminal domain to be preferentially and stoichiometrically assembled from two synthetic peptides (residues 93-126, SCIII, and 129-162, SCIV) in the presence of calcium only. It is therefore of great interest to know how closely the structure of this heterodimeric domain is to the intact protein domain. Analysis of such a structure has important implications in protein engineering and in understanding the stability of calcium-binding proteins in terms of biological function. The solution structure of this heterodimeric protein was determined by 1H NMR spectroscopy using 802 NOE derived distance restraints and 23 phi and 22 chi angle restraints. Distance geometry-simulated annealing calculations yielded a family of 42 converged structures (rmsd 0.86 +/- 0.17 A) showing an arrangement of four alpha-helices similar in fold to the C-terminal of troponin C. The dimer interface has several important interactions between helix pairs E/H and F/G responsible for the association of the two peptides. However, neither the peptide complex nor the solution NMR structure of TnC pack as tightly as that observed in the TnC X-ray structure. The interhelical distance between the F/G helix is about 1.4 A greater in solution than in the crystal. A comparison of the exposed surface area of the hydrophobic residues in the SCIII/SCIV heterodimer revealed that residues 1104, Y112, and 1121 are more exposed than in the previously determined solution structure of the SCIII homodimer. These residues are important for the interaction with the inhibitory region of TnI and provide evidence for their involvement in the regulation of muscle contraction.
-
-	NMR solution structure of a synthetic troponin C heterodimeric domain.,Shaw GS, Sykes BD Biochemistry. 1996 Jun 11;35(23):7429-38. PMID:8652520<ref>PMID:8652520</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1pon" 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: Shaw~~, G S~~]]	+	[[Category: Shaw GS]]
-	[[Category: Sykes~~, B D]]~~	+	[[Category: Sykes BD]]
-	~~[[Category: Calcium-binding protein]]~~	+
-	~~[[Category: Ef-hand]]~~	+
-	~~[[Category: Muscle protein~~]]	+

OCA at 09:32, 8 September 2021

OCA — Wed, 08 Sep 2021 09:32:43 GMT

←Older revision		Revision as of 09:32, 8 September 2021
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	<StructureSection load='1pon' size='340' side='right'caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>		<StructureSection load='1pon' size='340' side='right'caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PON FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PON FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [~~http~~://pdbe.org/1pon PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1pon PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1pon 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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [https://pdbe.org/1pon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [https://www.ebi.ac.uk/pdbsum/1pon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pon 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 09:46, 27 November 2019

OCA — Wed, 27 Nov 2019 09:46:06 GMT

←Older revision		Revision as of 09:46, 27 November 2019
Line 1:		Line 1:

	==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==		==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==
-	<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>	+	<StructureSection load='1pon' size='340' side='right'caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1pon" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pon" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Troponin\|Troponin]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Chick]]		[[Category: Chick]]
		+	[[Category: Large Structures]]
	[[Category: Shaw, G S]]		[[Category: Shaw, G S]]
	[[Category: Sykes, B D]]		[[Category: Sykes, B D]]

OCA at 07:53, 24 February 2018

OCA — Sat, 24 Feb 2018 07:53:06 GMT

←Older revision		Revision as of 07:53, 24 February 2018
Line 1:		Line 1:
		+
	==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==		==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==
	<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>		<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://pdbe.org/1pon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://pdbe.org/1pon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pon ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1pon_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1pon_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>
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	</div>		</div>
	<div class="pdbe-citations 1pon" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pon" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Troponin\|Troponin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:39, 9 February 2016

OCA — Tue, 09 Feb 2016 10:39:16 GMT

←Older revision		Revision as of 10:39, 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=1pon ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:27, 10 September 2015

OCA — Thu, 10 Sep 2015 21:27:59 GMT

←Older revision		Revision as of 21:27, 10 September 2015
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	<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>		<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://pdbe.org/1pon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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 1pon" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gallus gallus~~]]	+	[[Category: Chick]]
	[[Category: Shaw, G S]]		[[Category: Shaw, G S]]
	[[Category: Sykes, B D]]		[[Category: Sykes, B D]]

OCA at 06:19, 25 December 2014

OCA — Thu, 25 Dec 2014 06:19:29 GMT

←Older revision		Revision as of 06:19, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
-	[[Category: Shaw, G S.]]	+	[[Category: Shaw, G S]]
-	[[Category: Sykes, B D.]]	+	[[Category: Sykes, B D]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Ef-hand]]		[[Category: Ef-hand]]
	[[Category: Muscle protein]]		[[Category: Muscle protein]]

OCA at 23:42, 28 September 2014

OCA — Sun, 28 Sep 2014 23:42:37 GMT

←Older revision		Revision as of 23:42, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1pon.~~png\|left~~\|200px]]	+	==SITE III-SITE IV TROPONIN C HETERODIMER, NMR==
		+	<StructureSection load='1pon' size='340' side='right' caption='[[1pon]], [[NMR_Ensembles_of_Models \| 42 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1pon]] is a 2 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=1PON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PON FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pon OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pon RCSB], [http://www.ebi.ac.uk/pdbsum/1pon 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/po/1pon_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 C-terminal domain from the muscle protein troponin C (TnC) comprises two helix-loop-helix calcium-binding sites (residues 90-162). The assembly of these two sites is governed by calcium binding enabling a synthetic C-terminal domain to be preferentially and stoichiometrically assembled from two synthetic peptides (residues 93-126, SCIII, and 129-162, SCIV) in the presence of calcium only. It is therefore of great interest to know how closely the structure of this heterodimeric domain is to the intact protein domain. Analysis of such a structure has important implications in protein engineering and in understanding the stability of calcium-binding proteins in terms of biological function. The solution structure of this heterodimeric protein was determined by 1H NMR spectroscopy using 802 NOE derived distance restraints and 23 phi and 22 chi angle restraints. Distance geometry-simulated annealing calculations yielded a family of 42 converged structures (rmsd 0.86 +/- 0.17 A) showing an arrangement of four alpha-helices similar in fold to the C-terminal of troponin C. The dimer interface has several important interactions between helix pairs E/H and F/G responsible for the association of the two peptides. However, neither the peptide complex nor the solution NMR structure of TnC pack as tightly as that observed in the TnC X-ray structure. The interhelical distance between the F/G helix is about 1.4 A greater in solution than in the crystal. A comparison of the exposed surface area of the hydrophobic residues in the SCIII/SCIV heterodimer revealed that residues 1104, Y112, and 1121 are more exposed than in the previously determined solution structure of the SCIII homodimer. These residues are important for the interaction with the inhibitory region of TnI and provide evidence for their involvement in the regulation of muscle contraction.

-	~~{{STRUCTURE_1pon\| PDB=1pon \| SCENE= }}~~	+	NMR solution structure of a synthetic troponin C heterodimeric domain.,Shaw GS, Sykes BD Biochemistry. 1996 Jun 11;35(23):7429-38. PMID:8652520<ref>PMID:8652520</ref>

-	~~===SITE III-SITE IV TROPONIN C HETERODIMER~~, ~~NMR===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8652520}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1pon]] is~~ a ~~2 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=1PON OCA].~~	+

	==See Also==		==See Also==
	*[[Troponin\|Troponin]]		*[[Troponin\|Troponin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008652520<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Shaw, G S.]]		[[Category: Shaw, G S.]]

OCA at 13:36, 20 October 2012

OCA — Sat, 20 Oct 2012 13:36:23 GMT

←Older revision		Revision as of 13:36, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1pon]] is a 2 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=1PON OCA].	+	[[1pon]] is a 2 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=1PON OCA].

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

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

OCA — Thu, 26 Jul 2012 12:30:38 GMT

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

←Older revision

Revision as of 12:30, 26 July 2012