Phosphoproteins of the stathmin family interact with the alpha beta tubulin
heterodimer (tubulin) and hence interfere with microtubule dynamics. The s
tructure of the complex of GDP-tubulin with the stathmin-like domain of the
neural protein RB3 reveals a head-to-tail assembly of two tubulins with a
91-residue RB3 alpha helix in which each copy of an internal duplicated seq
uence interacts with a different tubulin. As a result of the relative orien
tations adopted by tubulins and by their alpha and beta subunits, the tubul
in:RB3 complex forms a curved structure. The RB3 helix thus most likely pre
vents incorporation of tubulin into microtubules by holding it in an assemb
ly with a curvature very similar to that of the depolymerization products o
f microtubules.