title: Construction of a model of the Candida albicans lanosterol 14-alpha-demethylase active site using the homology modelling technique.
abstract: On the basis of all hitherto known P450 X-ray structures and applying standard homology modelling procedures a three-dimensional model of the lanosterol-14 alpha-demethylase active site was constructed. The modelled active site nicely hosts the natural substrate lanosterol and the substrate-enzyme complex displayed stability in a 70 ps molecular dynamics simulation. The importance of Thr 122 of lanosterol 14 alpha-demethylase for hydrogen bond formation with the 3-hydroxyl group of lanosterol was found to be a characteristic feature of the interaction geometry.
authors.affiliation: Institute for Pharmaceutical Chemistry, Heinrich-Heine-Universität Düsseldorf, Germany.
authors.forename: H D
authors.initials: HD
authors.lastname: Höltje
authors.forename: C
authors.initials: C
authors.lastname: Fattorusso
mesh_terms: D001665:Binding Sites; D002176:Candida albicans / Q000201:enzymology*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D058886:Sterol 14-Demethylase
chemical_list: D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D058886:Sterol 14-Demethylase