1a2x

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[[Image:1a2x.jpg|left|200px]]
 
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==COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I==
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The line below this paragraph, containing "STRUCTURE_1a2x", creates the "Structure Box" on the page.
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<StructureSection load='1a2x' size='340' side='right'caption='[[1a2x]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1a2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2X 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">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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_1a2x| PDB=1a2x | 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=1a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2x OCA], [https://pdbe.org/1a2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2x RCSB], [https://www.ebi.ac.uk/pdbsum/1a2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TNNC2_RABIT TNNC2_RABIT] 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/a2/1a2x_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=1a2x ConSurf].
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<div style="clear:both"></div>
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'''COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I'''
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==See Also==
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*[[Troponin 3D structures|Troponin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Troponin (Tn), the complex of three subunits (TnC, TnI, and TnT), plays a key role in Ca2+-dependent regulation of muscle contraction. To elucidate the interactions between the Tn subunits and the conformation of TnC in the Tn complex, we have determined the crystal structure of TnC (two Ca2+ bound state) in complex with the N-terminal fragment of TnI (TnI1-47). The structure was solved by the single isomorphous replacement method in combination with multiple wavelength anomalous dispersion data. The refinement converged to a crystallographic R factor of 22.2% (Rfree = 32.6%). The central, connecting alpha-helix observed in the structure of uncomplexed TnC (TnCfree) is unwound at the center (residues Ala-87, Lys-88, Gly-89, Lys-90, and Ser-91) and bent by 90 degrees. As a result, TnC in the complex has a compact globular shape with direct interactions between the N- and C-terminal lobes, in contrast to the elongated dumb-bell shaped molecule of uncomplexed TnC. The 31-residue long TnI1-47 alpha-helix stretches on the surface of TnC and stabilizes its compact conformation by multiple contacts with both TnC lobes. The amphiphilic C-end of the TnI1-47 alpha-helix is bound in the hydrophobic pocket of the TnC C-lobe through 38 van der Waals interactions. The results indicate the major difference between Ca2+ receptors integrated with the other proteins (TnC in Tn) and isolated in the cytosol (calmodulin). The TnC/TnI1-47 structure implies a mechanism of how Tn regulates the muscle contraction and suggests a unique alpha-helical regulatory TnI segment, which binds to the N-lobe of TnC in its Ca2+ bound conformation.
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[[Category: Large Structures]]
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==About this Structure==
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1A2X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2X OCA].
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==Reference==
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Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution., Vassylyev DG, Takeda S, Wakatsuki S, Maeda K, Maeda Y, Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4847-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9560191 9560191]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
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[[Category: Maeda K]]
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[[Category: Maeda, K.]]
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[[Category: Maeda Y]]
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[[Category: Maeda, Y.]]
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[[Category: Takeda S]]
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[[Category: Takeda, S.]]
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[[Category: Vassylyev DG]]
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[[Category: Vassylyev, D G.]]
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[[Category: Wakatsuki S]]
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[[Category: Wakatsuki, S.]]
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[[Category: Muscle contraction regulation]]
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[[Category: Troponin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:43:42 2008''
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Current revision

COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I

PDB ID 1a2x

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