Exploring the Origin of Differential Binding Affinities of Human Tubulin Isotypes αβII, αβIII and αβIV for DAMA-Colchicine Using Homology Modelling, Molecular Docking and Molecular Dynamics Simulations
Fig 6
Molecular dynamics (MD) simulated end structures of tubulin 1SA0 and tubulin isotypes.
The positions of DAMA-colchicine before and after simulation are shown for comparison. The colour scheme for αβ-tubulin and DAMA-colchicine is same as for the Fig 3. Initial docked conformation of DAMA-colchicine (before simulation) shown in magenta colour while DAMA-colchicine after simulation is shown in green colour similar to Fig 3. (A) Tubulin 1SA0 and DAMA-colchicine complex. (B) αβII tubulin isotype-DAMA-colchicine complex. (C) αβIII tubulin isotype-DAMA-colchicine complex (D) αβIV tubulin isotype-DAMA-colchicine complex. It is observed after simulation that the DAMA-colchicine moves away from the initial position in αβIII tubulin isotype.