The Free Energy Profile of Tubulin Straight-Bent Conformational Changes, with Implications for Microtubule Assembly and Drug Discovery
Figure 6
The colchicine binding pocket is sterically constrained in tubulin conformations with lower curvature.
a) Ratios of the volume of colchicine with respect to the volume of the predicted binding pocket for representative colchicine-bound tubulin heterodimers with curvatures of θ∼0°, 2°, 6°, 8°, 10°, and 12°. b) SiteMap predictions of the colchicine binding site for colchicine-bound tubulin structures with intradimer curvature of θ = 0°, 2°, 6°, 8°, 10°, and 12°. For each colchicine-bound tubulin structure, the representative structure with the maximum SiteScore is displayed. Black dots represent the predicted binding pocket of colchicine. Structural elements comprising the colchicine-binding domain are rendered as cartoon.