Variations in the colchicine-binding domain provide insight into the structural switch of tubulin.

ABSTRACT: Structural changes occur in the alphabeta-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to a curved structure. There is a broad range of small molecule compounds that disturbs the microtubule cycle, a class of which targets the colchicine-binding site and prevents microtubule assembly. This class includes compounds with very different chemical structures, and it is presently unknown whether they prevent tubulin polymerization by the same mechanism. To address this issue, we have determined the structures of tubulin complexed with a set of such ligands and show that they interfere with several of the movements of tubulin subunits structural elements upon its transition from curved t

SUBMITTER: Dorleans A 

PROVIDER: S-EPMC2728970 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature