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This observation has led to the conclusion that the most accurate predicted molecular model of calmodulin would be based on the X\u2010ray crystallographic coordinates of the highly refined structure of turkey skeletal troponin\u2010C. 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\u2010bonded contacts. In the analysis of the resulting structure, many features of calmodulin, including the detailed conformation of the Ca<jats:sup>2+<\/jats:sup>\u2010binding loops, the amino\u2010 and carboxy\u2010terminal hydrophobic patches of the Ca<jats:sup>2+<\/jats:sup>\u2010bound form, and the several clusters of acidic residues can be reconciled with much of the previously published solution data. Calmodulin in missing the N\u2010terminal helix characteristic of troponin\u2010C. The deletion of three residues from the central helical linker (denoted D\/E in troponin\u2010D) shortens the molecule and changes the orientation of the two domains of calmodulin by 60\u00b0 relative to those in troponin\u2010C. The molecular model has been used to derive two possible binding sites for the antipsychotic drug trifluoperazine, a potent competitive inhibitor of calmodulin activity.<\/jats:p>","DOI":"10.1002\/prot.340030102","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T01:07:03Z","timestamp":1117242423000},"page":"1-17","source":"Crossref","is-referenced-by-count":71,"title":["Two trifluoperazine\u2010binding sites on calmodulin predicted from comparative molecular modeling with troponin\u2010C"],"prefix":"10.1002","volume":"3","author":[{"given":"Natalie C. J.","family":"Strynadka","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael N. 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