Comparative Analyses of the β-Tubulin Gene and Molecular Modeling Reveal Molecular Insight into the Colchicine Resistance in Kinetoplastids Organisms

Figure 2

Amino acid residues sequence and secondary structure of the β-tubulin colchicine-binding domains. The amino acid residues sequence of the β-tubulin colchicine-binding domains I, II, and III of different organisms were aligned and compared to visualize amino acid substitutions (AAS) generated by single nucleotide mutations; eleven AAS were labeled and cited in the text and Table 1. Identical amino acid residues are indicated by points.