The 4 Å X-ray structure of a tubulin:stathmin-like domain complex

被引:217
作者
Gigant, B
Curmi, PA
Martin-Barbey, C
Charbaut, E
Lachkar, S
Lebeau, L
Siavoshian, S
Sobel, A
Knossow, M
机构
[1] Lab Enzymol & Biochim Struct, CNRS, UPR 9063, F-91198 Gif Sur Yvette, France
[2] Inst Fer Moulin, INSERM, U440, F-75005 Paris, France
[3] Fac Pharm, CNRS, UMR 7514, F-67401 Illkirch Graffenstaden, France
关键词
D O I
10.1016/S0092-8674(00)00069-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phosphoproteins of the stathmin family interact with the alpha beta 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.
引用
收藏
页码:809 / 816
页数:8
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