1jc2

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[[Image:1jc2.png|left|200px]]
 
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==COMPLEX OF THE C-DOMAIN OF TROPONIN C WITH RESIDUES 1-40 OF TROPONIN I==
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The line below this paragraph, containing "STRUCTURE_1jc2", creates the "Structure Box" on the page.
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<StructureSection load='1jc2' size='340' side='right'caption='[[1jc2]]' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jc2]] 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=1JC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JC2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_1jc2| PDB=1jc2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc2 OCA], [https://pdbe.org/1jc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1jc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jc2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jc/1jc2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1jc2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the calcium-saturated C-domain of skeletal troponin C (CTnC) in complex with a regulatory peptide comprising residues 1-40 (Rp40) of troponin I (TnI) was determined using nuclear magnetic resonance (NMR) spectroscopy. The solution structure determined by NMR is similar to the structure of the C-domain from intact TnC in complex with TnI(1)(-)(47) determined by X-ray crystallography [Vassylyev, D. G., Takeda, S., Wakatsuki, S., Maeda, K., and Maeda, Y. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852]. Changes in the dynamic properties of CTnC.2Ca2+ induced by Rp40 binding were investigated using backbone amide (15)N NMR relaxation measurements. Analysis of NMR relaxation data allows for extraction of motional order parameters on a per residue basis, from which the contribution of changes in picosecond to nanosecond time scale motions to the conformational entropy associated with complex formation can be estimated. The results indicate that binding of Rp40 decreases backbone flexibility in CTnC, particularly at the end of the C-terminal helix. The backbone conformational entropy change (-TDeltaS) associated with binding of Rp40 to CTnC.2Ca2+ determined from (15)N relaxation data is 9.6 +/- 0.7 kcal mol(-1) at 30 degrees C. However, estimation of thermodynamic quantities using a structural approach [Lavigne, P., Bagu, J. R., Boyko, R., Willard, L., Holmes, C. F., and Sykes, B. D. (2000) Protein Sci. 9, 252-264] reveals that the change in solvation entropy upon complex formation is dominant and overcomes the thermodynamic "cost" associated with "stiffening" of the protein backbone upon Rp40 binding. Additionally, backbone amide (15)N relaxation data measured at different concentrations of CTnC.2Ca2+.Rp40 reveal that the complex dimerizes in solution. Fitting of the apparent global rotational correlation time as a function of concentration to a monomer-dimer equilibrium yields a dimerization constant of approximately 8.3 mM.
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===COMPLEX OF THE C-DOMAIN OF TROPONIN C WITH RESIDUES 1-40 OF TROPONIN I===
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Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I.,Mercier P, Spyracopoulos L, Sykes BD Biochemistry. 2001 Aug 28;40(34):10063-77. PMID:11513585<ref>PMID:11513585</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1jc2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11513585}}, adds the Publication Abstract to the page
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*[[Troponin 3D structures|Troponin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11513585 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11513585}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1JC2 is a [[Single protein]] structure of 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=1JC2 OCA].
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==Reference==
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Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I., Mercier P, Spyracopoulos L, Sykes BD, Biochemistry. 2001 Aug 28;40(34):10063-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11513585 11513585]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Mercier, P.]]
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[[Category: Mercier P]]
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[[Category: Spyracopoulos, L.]]
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[[Category: Spyracopoulos L]]
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[[Category: Sykes, B D.]]
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[[Category: Sykes BD]]
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[[Category: Ca2+ binding protein]]
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[[Category: Muscle contraction]]
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[[Category: Troponin c]]
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[[Category: Troponin i]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:00:11 2008''
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Current revision

COMPLEX OF THE C-DOMAIN OF TROPONIN C WITH RESIDUES 1-40 OF TROPONIN I

PDB ID 1jc2

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