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 2
Multiple sequence analysis of tubulin 1SA0 and human β-tubulin isotypes.
The isotype βIII shows change of Ala315 to Thr, Cys239 to Ser, and Thr351-to Val, Isotype βII change of Val316 to Ile at the colchicine binding pocket. Region of changed residues at colchicine binding pocket are shown in red color.