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

<table>Multiple alignments of the β-tubulin protein of different organisms. Predicted amino acid sequences of Leishmania (Viannia) guyanensis M4147 (accession number ABG91756), L. (Leishmania) major (accession number. XP_001681156), L. tarentolae (accession number ABC40567), Trypanosoma cruzi (accession number AAL75956), T. brucei (accession number XP_001218933), human (accession number AAB59507), B. taurus. (accession number. NP_001003900), and A. polyphaga (accession number AAZ80769) were aligned by the CLUSTAL software. Amino acid residues involved in structural domain previously assigned to the ligands colchicine are indicated as regions I (position 240–260), II (position 309–321) and III (position 347–360). </table>

BioMed Research International

fig1

Figure 1

Figure 1: Comparative Analyses of the β-Tubulin Gene and Molecular Modeling Reveal Molecular Insight into the Colchicine Resistance in Kinetoplastids Organisms

Figure 1 | Comparative Analyses of the β-Tubulin Gene and Molecular Modeling Reveal Molecular Insight into the Colchicine Resistance in Kinetoplastids Organisms 