2cln: Difference between revisions

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 {{Theoretical_model}}
-[[Image:2cln.png|left|200px]]
+==TWO TRIFLUOPERAZINE-BINDING SITES ON CALMODULIN PREDICTED FROM COMPARATIVE MOLECULAR MODELLING WITH TROPONIN-C==
+<StructureSection load='2cln' size='340' side='right'caption='[[2cln]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLN FirstGlance]. <br>
+</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=2cln FirstGlance], [https://www.ebi.ac.uk/pdbsum/2cln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cln ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Among the known regulatory proteins that are conformationally sensitive to the binding of calcium ions, calmodulin and troponin-C have the greatest primary sequence homology. This observation has led to the conclusion that the most accurate predicted molecular model of calmodulin would be based on the X-ray crystallographic coordinates of the highly refined structure of turkey skeletal troponin-C. This paper describes the structure of calmodulin built from such a premise. The resulting molecular model was subjected to conjugate gradient energy minimization to remove unacceptable intramolecular non-bonded contacts. In the analysis of the resulting structure, many features of calmodulin, including the detailed conformation of the Ca2+-binding loops, the amino- and carboxy-terminal hydrophobic patches of the Ca2+-bound form, and the several clusters of acidic residues can be reconciled with much of the previously published solution data. Calmodulin is missing the N-terminal helix characteristic of troponin-C. The deletion of three residues from the central helical linker (denoted D/E in troponin-C) shortens the molecule and changes the orientation of the two domains of calmodulin by 60 degrees relative to those in troponin-C. The molecular model has been used to derive two possible binding sites for the antipsychotic drug trifluoperazine, a potent competitive inhibitor of calmodulin activity.
-{{STRUCTURE_2cln|  PDB=2cln  |  SCENE=  }}
+Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C.,Strynadka NC, James MN Proteins. 1988;3(1):1-17. PMID:3375233<ref>PMID:3375233</ref>
-===TWO TRIFLUOPERAZINE-BINDING SITES ON CALMODULIN PREDICTED FROM COMPARATIVE MOLECULAR MODELLING WITH TROPONIN-C===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_3375233}}
+<div class="pdbe-citations 2cln" style="background-color:#fffaf0;"></div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:003375233</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Theoretical Model]]
+[[Category: Large Structures]]
 [[Category: James, M N.G]]
 [[Category: Strynadka, N C.J]]