1ctd: Difference between revisions

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-[[Image:1ctd.png|left|200px]]
-{{STRUCTURE_1ctd|  PDB=1ctd  |  SCENE=  }}
+==DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY==
+<StructureSection load='1ctd' size='340' side='right'caption='[[1ctd]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ctd]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 7 models</td></tr>
+<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ctd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctd OCA], [https://pdbe.org/1ctd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ctd RCSB], [https://www.ebi.ac.uk/pdbsum/1ctd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctd 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/ct/1ctd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ctd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium this peptide forms a symmetric two-site homodimeric calcium-binding domain (Shaw et al., 1990). The solution structure of this dimer was determined from the measurement of 470 NOEs from a 75-ms NOESY data set. For the dimer structure determination, the constraint list included 868 distance restraints, 44 phi angles, and 24 chi 1 and 2 chi 2 angles. Seven structures were calculated by restrained molecular dynamics using a procedure in which intramonomer distances were used first and then all distances, intra- and intermonomer, were input during further dynamics. The structures exhibited a fold very similar to the C-terminal domain of troponin-C comprised of a pair of helix-loop-helix calcium-binding sites. The rms deviation of these structures for backbone atoms between residues 97-122 and 97'-122' for the dimer was 0.82 A. The dimer structure was also calculated to be more symmetric than sites III and IV in troponin-C.
-===DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY===
+Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.,Shaw GS, Hodges RS, Sykes BD Biochemistry. 1992 Oct 13;31(40):9572-80. PMID:1390738<ref>PMID:1390738</ref>
-{{ABSTRACT_PUBMED_1390738}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1ctd" style="background-color:#fffaf0;"></div>
-[[1ctd]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTD OCA].
 ==See Also==
-*[[Troponin|Troponin]]
+*[[Troponin 3D structures|Troponin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:001390738</ref><references group="xtra"/>
+__TOC__
-[[Category: Shaw, G S.]]
+</StructureSection>
-[[Category: Sykes, B D.]]
+[[Category: Large Structures]]
-[[Category: Muscle protein]]
+[[Category: Shaw GS]]
+[[Category: Sykes BD]]