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微管蛋白与类stathmin结构域复合物的4A X射线结构。

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

作者信息

Gigant B, Curmi P A, Martin-Barbey C, Charbaut E, Lachkar S, Lebeau L, Siavoshian S, Sobel A, Knossow M

机构信息

Laboratoire d'Enzymologie et Biochimie Structurales CNRS UPR 9063, Gif sur Yvette, France.

出版信息

Cell. 2000 Sep 15;102(6):809-16. doi: 10.1016/s0092-8674(00)00069-6.

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.

摘要

信号素家族的磷蛋白与αβ微管蛋白异二聚体(微管蛋白)相互作用,从而干扰微管动力学。GDP-微管蛋白与神经蛋白RB3的信号素样结构域形成的复合物结构揭示了两个微管蛋白的头对头组装,中间有一个91个残基的RB3α螺旋,其中内部重复序列的每个拷贝与不同的微管蛋白相互作用。由于微管蛋白及其α和β亚基所采用的相对取向,微管蛋白:RB3复合物形成了一种弯曲结构。因此,RB3螺旋很可能通过将微管蛋白保持在一种曲率与微管解聚产物非常相似的组装状态,从而阻止微管蛋白掺入微管。

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