Title of article
The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex
Author/Authors
Benoît Gigant، نويسنده , , Patrick A. Curmi، نويسنده , , Carole Martin-Barbey، نويسنده , , Elodie Charbaut، نويسنده , , Sylvie Lachkar، نويسنده , , Luc Lebeau، نويسنده , , Samila Siavoshian، نويسنده , , André Sobel، نويسنده , , Marcel Knossow، نويسنده ,
Issue Information
هفته نامه با شماره پیاپی سال 2000
Pages
8
From page
809
To page
816
Abstract
Phosphoproteins of the stathmin family interact with the αβ 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 α 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 α and β 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.
Journal title
CELL
Serial Year
2000
Journal title
CELL
Record number
1017103
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