To date the structure of hFMO3 has not been solved due to difficulties in the crystallization of microsomal, membrane-bound proteins [9]. In 1991 Ozols [10] revealed that the C-terminus of FMO2 is very hydrophobic and it could anchor the protein to the membrane. Recently, Krueger and co-workers [11] reported on the expression and purification attempts of a soluble rabbit FMO2 by deleting 26 amino acids from the C-terminus region presumed to function as the membrane anchor. In the present study a molecular model of hFMO3 is constructed, exploited for molecular dynamics experiments to identify the membrane insertion mechanism and used as the in silico basis for the rational design of a soluble truncated hFMO3 enzyme.
Molecular modelling of human flavin-containing monooxygenase 3
CATUCCI, GIANLUCA;SADEGHI, JILA;GILARDI, Gianfranco
2013-01-01
Abstract
To date the structure of hFMO3 has not been solved due to difficulties in the crystallization of microsomal, membrane-bound proteins [9]. In 1991 Ozols [10] revealed that the C-terminus of FMO2 is very hydrophobic and it could anchor the protein to the membrane. Recently, Krueger and co-workers [11] reported on the expression and purification attempts of a soluble rabbit FMO2 by deleting 26 amino acids from the C-terminus region presumed to function as the membrane anchor. In the present study a molecular model of hFMO3 is constructed, exploited for molecular dynamics experiments to identify the membrane insertion mechanism and used as the in silico basis for the rational design of a soluble truncated hFMO3 enzyme.File | Dimensione | Formato | |
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