Structural insights into microtubule function.

By E. Nogales. Annual Review of Biochemistry, 2000

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High resolution microtubule structures reveal the structural transitions in αβ–tubulin upon GTP hydrolysis (2014, background): “The nucleotide at the E-site (exchangeable) in b-tubulin is exposed on the surface of an unpolymerized dimer and the terminal subunits of a microtubule plus end (Mitchison, 1993; Nogales, 2000).”
Dinitroanilines Bind α-Tubulin to Disrupt Microtubules (2004, background): “This is unusual, as all characterized compounds that perturb microtubule function bind to and act on -tubulin (Nogales, 2000).”
Microtubules as a target for anticancer drugs (2004, background): “A generally accepted model in the field is that tubulin–GTP polymerizes into protofilaments that have a straight conformation, but that following GTP hydrolysis, the tubulin conformation changes to a curved form, such that the tubulin–GDP that is locked into the microtubule core is in a strained con”
Mechanisms of Taxol resistance related to microtubules (2003, background): “The M-loop has also been implicated in the unusual cold stability of Antarctic fish tubulin (Detrich et al., 2000).”
Microtubule assembly, organization and dynamics in axons and dendrites (2009, background): “This is known as dynamic instability and has been observed both in vitro and in vivo”