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1cta

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[[Image:1cta.png|left|200px]]
 
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{{STRUCTURE_1cta| PDB=1cta | SCENE= }}
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==DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY==
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<StructureSection load='1cta' size='340' side='right'caption='[[1cta]]' scene=''>
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===DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cta]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTA FirstGlance]. <br>
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{{ABSTRACT_PUBMED_1390738}}
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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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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==About this Structure==
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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=1cta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cta OCA], [https://pdbe.org/1cta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cta RCSB], [https://www.ebi.ac.uk/pdbsum/1cta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cta ProSAT]</span></td></tr>
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[[1cta]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTA OCA].
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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/ct/1cta_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=1cta ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Troponin|Troponin]]
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*[[Troponin 3D structures|Troponin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:001390738</ref><references group="xtra"/>
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[[Category: Large Structures]]
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[[Category: Shaw, G S.]]
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[[Category: Shaw GS]]
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[[Category: Sykes, B D.]]
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[[Category: Sykes BD]]
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[[Category: Muscle protein]]
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Current revision

DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY

PDB ID 1cta

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