1yv0

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[[Image:1yv0.jpg|left|200px]]
 
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==Crystal structure of skeletal muscle troponin in the Ca2+-free state==
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The line below this paragraph, containing "STRUCTURE_1yv0", creates the "Structure Box" on the page.
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<StructureSection load='1yv0' size='340' side='right'caption='[[1yv0]], [[Resolution|resolution]] 7.00&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'>[[1yv0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YV0 FirstGlance]. <br>
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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]] 7&#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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1yv0| PDB=1yv0 | 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=1yv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv0 OCA], [https://pdbe.org/1yv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1yv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yv0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TNNT3_CHICK TNNT3_CHICK] Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
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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/yv/1yv0_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=1yv0 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of skeletal muscle troponin in the Ca2+-free state'''
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==See Also==
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*[[Troponin|Troponin]]
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*[[Troponin 3D structures|Troponin 3D structures]]
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==Overview==
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__TOC__
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Troponin senses Ca2+ to regulate contraction in striated muscle. Structures of skeletal muscle troponin composed of TnC (the sensor), TnI (the regulator), and TnT (the link to the muscle thin filament) have been determined. The structure of troponin in the Ca(2+)-activated state features a nearly twofold symmetrical assembly of TnI and TnT subunits penetrated asymmetrically by the dumbbell-shaped TnC subunit. Ca ions are thought to regulate contraction by controlling the presentation to and withdrawal of the TnI inhibitory segment from the thin filament. Here, we show that the rigid central helix of the sensor binds the inhibitory segment of TnI in the Ca(2+)-activated state. Comparison of crystal structures of troponin in the Ca(2+)-activated state at 3.0 angstroms resolution and in the Ca(2+)-free state at 7.0 angstroms resolution shows that the long framework helices of TnI and TnT, presumed to be a Ca(2+)-independent structural domain of troponin are unchanged. Loss of Ca ions causes the rigid central helix of the sensor to collapse and to release the inhibitory segment of TnI. The inhibitory segment of TnI changes conformation from an extended loop in the presence of Ca2+ to a short alpha-helix in its absence. We also show that Anapoe, a detergent molecule, increases the contractile force of muscle fibers and binds specifically, together with the TnI switch helix, in a hydrophobic pocket of TnC upon activation by Ca ions.
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</StructureSection>
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==About this Structure==
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1YV0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YV0 OCA].
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==Reference==
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Ca(2+)-regulated structural changes in troponin., Vinogradova MV, Stone DB, Malanina GG, Karatzaferi C, Cooke R, Mendelson RA, Fletterick RJ, Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5038-43. Epub 2005 Mar 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15784741 15784741]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Cooke, R.]]
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[[Category: Cooke R]]
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[[Category: Fletterick, R J.]]
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[[Category: Fletterick RJ]]
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[[Category: Karatzaferi, C.]]
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[[Category: Karatzaferi C]]
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[[Category: Malanina, G G.]]
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[[Category: Malanina GG]]
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[[Category: Mendelson, R A.]]
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[[Category: Mendelson RA]]
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[[Category: Stone, D B.]]
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[[Category: Stone DB]]
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[[Category: Vinogradova, M V.]]
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[[Category: Vinogradova MV]]
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[[Category: Actin binding]]
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[[Category: Muscle]]
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[[Category: Off state]]
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[[Category: Thin filament]]
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[[Category: Troponin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:49:19 2008''
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Current revision

Crystal structure of skeletal muscle troponin in the Ca2+-free state

PDB ID 1yv0

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