[Computer modeling of the human cytochrome P-450 2E1 complex formation]

A comparison has been made between spatial structures of human CYP2E1 obtained experimentally and those calculated using the computer methods. The structures were characterized by such parameters as total energy, protein pocket volume and total volume of molecules as well as the analysis of spatial geometry. The obtained results have proved that the model calculated and optimized by us can be used for studing the mechanisms of interaction of the active center of the enzyme with substrates and inhibitors. An assumption was made in the course of the research that one of the possible mechanisms of inactivation of the enzyme is the reduction of protein pocket volume, which prevents substrate access to the active center.