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The 4 A X-ray structure of a tubulin:stathmin-like domain complex
Authors:Gigant B  Curmi P A  Martin-Barbey C  Charbaut E  Lachkar S  Lebeau L  Siavoshian S  Sobel A  Knossow M
Affiliation:Laboratoire d'Enzymologie et Biochimie Structurales CNRS UPR 9063, Gif sur Yvette, France.
Abstract:Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure 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 sequence interacts with a different tubulin. As a result of the relative orientations adopted by tubulins and by their alpha and beta subunits, the tubulin:RB3 complex forms a curved structure. The RB3 helix thus most likely prevents incorporation of tubulin into microtubules by holding it in an assembly with a curvature very similar to that of the depolymerization products of microtubules.
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