Comparison of the predicted binding models of mHA1, mHA6, and mHA 11 to the tubulin protein with that of DAMA-colchicine in the crystal structure. Comparison.

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Comparison of the predicted binding models of mHA1, mHA6, and mHA 11 to the tubulin protein with that of DAMA-colchicine in the crystal structure. Comparison of the predicted binding models of mHA1, mHA6, and mHA 11 to the tubulin protein with that of DAMA-colchicine in the crystal structure. A, mHA1 and mHA6 bind to the colchicine-binding site in the same manner. B, the binding modes of mHA1 and mHA11 differ slightly. Carbon atoms in mHA1, mHA6, and mHA11 are shown as sticks; and DAMA-colchicine as lines. The carbon atoms are colored in magenta for mHA1, in orange for mHA6, in deep teal for mHA11, and in cyan for DAMA-colchicine. Nitrogen and oxygen atoms are colored in blue and red, respectively. These figures were rendered using Pymol. Jingle Xi et al. Mol Cancer Res 2013;11:856-864 ©2013 by American Association for Cancer Research