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==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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CLN FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cln FirstGlance], [http://www.ebi.ac.uk/pdbsum/2cln PDBsum]</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: James, M N.G]] | [[Category: James, M N.G]] | ||
[[Category: Strynadka, N C.J]] | [[Category: Strynadka, N C.J]] | ||
Revision as of 08:55, 29 September 2014
TWO TRIFLUOPERAZINE-BINDING SITES ON CALMODULIN PREDICTED FROM COMPARATIVE MOLECULAR MODELLING WITH TROPONIN-CTWO TRIFLUOPERAZINE-BINDING SITES ON CALMODULIN PREDICTED FROM COMPARATIVE MOLECULAR MODELLING WITH TROPONIN-C
Structural highlights
Publication Abstract from PubMedAmong 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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