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[[Image:1avs.jpg|left|200px]]


{{Structure
==X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C==
|PDB= 1avs |SIZE=350|CAPTION= <scene name='initialview01'>1avs</scene>, resolution 1.75&Aring;
<StructureSection load='1avs' size='340' side='right'caption='[[1avs]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[1avs]] is a 2 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=1AVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVS FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
|GENE=  
<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'>[https://proteopedia.org/fgij/fg.htm?mol=1avs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avs OCA], [https://pdbe.org/1avs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avs RCSB], [https://www.ebi.ac.uk/pdbsum/1avs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avs ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1avs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1avs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.


'''X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C'''
Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution.,Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:9367759<ref>PMID:9367759</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1avs" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.
*[[Troponin 3D structures|Troponin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1AVS is a [[Single protein]] structure of sequence 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=1AVS OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution., Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN, J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9367759 9367759]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: James, M N.G.]]
[[Category: James MNG]]
[[Category: Strynadka, N C.J.]]
[[Category: Strynadka NCJ]]
[[Category: CA]]
[[Category: calcium-activated]]
[[Category: e-f hand calcium-binding protein]]
[[Category: muscle contraction]]
[[Category: troponin]]
 
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