Determination of the optimal tubulin isotype target as a method for the development of individualized cancer chemotherapy

Table 1 Residue changes between β-tubulin isotypes in the binding sites for well-known drugs

Isotype	Residue changes in the paclitaxel binding site
βIII				S275A
βVI	V23M	S25G	D26E	S275A	R276Q
Isotype	Residue changes in the colchicine binding site
βIII		C239S			A315T	T351V
βV		C239S			A315T	T351V
βVI	V236I	C239S			A315T	T351V
Isotype	Residue changes in the vinblastine binding site
βIII				T218A

Residue changes between tubulin isotypes compared to βI tubulin with respect to the interactions with three well-known spindle poisons: paclitaxel, colchicine and vinblastine. Only residue differences in the respective binding sites are shown.

ISSN: 1742-4682