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| | ==STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES== | | ==STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES== |
| - | <StructureSection load='2ctn' size='340' side='right' caption='[[2ctn]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2ctn' size='340' side='right'caption='[[2ctn]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ctn]] 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=2CTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CTN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ctn]] 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=2CTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CTN 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTNC(A-CYS) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=2ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ctn OCA], [http://pdbe.org/2ctn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ctn RCSB], [http://www.ebi.ac.uk/pdbsum/2ctn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ctn 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=2ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ctn OCA], [https://pdbe.org/2ctn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ctn RCSB], [https://www.ebi.ac.uk/pdbsum/2ctn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ctn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TNNC1_CHICK TNNC1_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/TNNC1_CHICK TNNC1_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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| | ==See Also== | | ==See Also== |
| - | *[[Troponin|Troponin]] | + | *[[Troponin 3D structures|Troponin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Gagne, S M]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, M X]] | + | [[Category: Gagne SM]] |
| - | [[Category: Liu, W]] | + | [[Category: Li MX]] |
| - | [[Category: Putkey, J A]] | + | [[Category: Liu W]] |
| - | [[Category: Sia, S K]] | + | [[Category: Putkey JA]] |
| - | [[Category: Spyracopoulos, L]] | + | [[Category: Sia SK]] |
| - | [[Category: Sykes, B D]] | + | [[Category: Spyracopoulos L]] |
| - | [[Category: Calcium-binding protein]]
| + | [[Category: Sykes BD]] |
| - | [[Category: Cardiac]]
| + | |
| - | [[Category: Muscle]]
| + | |
| - | [[Category: Regulatory]]
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| Structural highlights
Function
TNNC1_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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.
Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain.,Sia SK, Li MX, Spyracopoulos L, Gagne SM, Liu W, Putkey JA, Sykes BD J Biol Chem. 1997 Jul 18;272(29):18216-21. PMID:9218458[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sia SK, Li MX, Spyracopoulos L, Gagne SM, Liu W, Putkey JA, Sykes BD. Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain. J Biol Chem. 1997 Jul 18;272(29):18216-21. PMID:9218458
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