| Literature DB >> 11030624 |
B Gigant1, P A Curmi, C Martin-Barbey, E Charbaut, S Lachkar, L Lebeau, S Siavoshian, A Sobel, M Knossow.
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.Entities:
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Year: 2000 PMID: 11030624 DOI: 10.1016/s0092-8674(00)00069-6
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582