Figure 3

3D structure-based models of the Eg5 complexes after the MD assays. Molecular dynamics simulations (MD) of the Eg5 protein and Eg5 protein complexes with each of the five tested compounds were conducted to assess the DHMPs influence on Eg5 movements. The panels show ribbon representations of the Eg5 and Licorice representations of the tested compounds and monastrol. The yellow dotted lines show the polar contacts responsible for the maintenance of molecule linkage with the protein binding-site. The binding-region is perfectly conserved, but not the binding-residues, which lead us to realize the influence of the compound topology. Major differences may be seen in the interactions between 4 m, 4x and 4p and the Eg5 binding-site, which show completely different binding-residues. However, 4bt and 4bc retain the linkage with the Arg119 of the Eg5 when comparing to the monastrol, showing its importance in the inhibition processes. Indirect links mediated by water molecules (cyan), occur in residues (green) annotated in orange; direct links occur with residues annotated in black.