On the basis of all hitherto known P450 X-ray structures and applying standard homology modelling procedures a three-dimensional model of the lanosterol-14α-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 14α-demethylase for hydrogen bond formation with the 3-hydroxyl group of lanosterol was found to be a characteristic feature of the interaction geometry.
Construction of a model of the Candida albicans lanosterol 14-alpha-demethylase active site using homology modelling technique / Hoeltje, H. D.; Fattorusso, Caterina. - In: PHARMACEUTICA ACTA HELVETIAE. - ISSN 0031-6865. - 72:(1998), pp. 271-277. [10.1016/S0031-6865(97)00036-8]
Construction of a model of the Candida albicans lanosterol 14-alpha-demethylase active site using homology modelling technique
FATTORUSSO, CATERINA
1998
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-14α-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 14α-demethylase for hydrogen bond formation with the 3-hydroxyl group of lanosterol was found to be a characteristic feature of the interaction geometry.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
