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Comparison of Multiple Molecular Dynamics Trajectories Calculated for the Drug-Resistant HIV-1 Integrase T661/M154I Catalytic Domain

Alessandro Brigo (Dipartimento di Scienze Farmaceutiches, Universit? degli Studi di Padova, 35131 Padova, Italy) , Lee, Keun-Woo (Department of Biology and Biochemistry, University of Houston, Houston, Texas 77024-5001) , Gabriela lurcu Mustata (Department of Biology and Biochemistry, University of Houston, Houston, Texas 77024-5001) , James M. Briggs (Department of Biology and Biochemistry, University of Houston, Houston, Texas 77024-5001)

Plant molecular biology and biotechnology research center Annual report, 2005, 2005, 181-191

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HIV-1 integrase (IN) is an essential enzyme for the viral replication and an intersting target for the design of new pharmaceuticals for multidrug therapy of AIDS. Single and multiple mutations of IN at residues T66, S153, or M154 confer degrees of resistance to several inhibitors that prevent the e...
HIV-1 integrase (IN) is an essential enzyme for the viral replication and an intersting target for the design of new pharmaceuticals for multidrug therapy of AIDS. Single and multiple mutations of IN at residues T66, S153, or M154 confer degrees of resistance to several inhibitors that prevent the enzyme from performing its normal strand transfer activity. Four different conformations of IN were chosen from a prior molecular dynamics (MD) simulation on the modeled IN T66I/M154I catalytic core domain as starting points for additional MD studies. The aim of this article is to understand the dynamic features that may play roles in the catalytic activity of the double mutant enzyme in the absence of any inhibitor. Moreover, we want to verify the trajectories obtained from these MD simulations we have demonstrated that the starting point does not affect the conformational space explored by this protein and that the time of the simulation is long enough to achieve convergence for this system.