ON THE STRUCTURE OF MICROTUBULES, TAU, AND PAIRED HELICAL FILAMENTS

被引:52
|
作者
MANDELKOW, E [1 ]
SONG, YH [1 ]
SCHWEERS, O [1 ]
MARX, A [1 ]
MANDELKOW, EM [1 ]
机构
[1] MAX PLANCK UNIT STRUCT MOLEC BIOL, D-22603 HAMBURG, GERMANY
关键词
MICROTUBULES; ALZHEIMERS DISEASE; PAIRED HELICAL FILAMENTS; TAU-PROTEIN; KINESIN; TUBULIN; X-RAY DIFFRACTION; ELECTRON MICROSCOPY;
D O I
10.1016/0197-4580(95)00026-B
中图分类号
R592 [老年病学]; C [社会科学总论];
学科分类号
03 ; 0303 ; 100203 ;
摘要
Microtubules and their associated proteins form the basis of axonal transport; they are degraded during the neuronal degeneration in Alzheimer's disease. This article surveys recent results on the structure of microtubules, tau protein, and PHFs. Microtubules have been investigated by electron microscopy and image processing after labeling them with the head domain of the motor protein kinesin. This reveals the arrangement of tubulin subunits in microtubules and the shape of the tubulin-motor complex. Tau protein was studied by electron microscopy, solution X-ray scattering, and spectroscopic methods. It appears as an elongated molecule (about 35 nm) without recognizable secondary structure. Alzheimer PHFs were examined by FTIR and X-ray diffraction; they, too, show evidence for secondary structure such as beta sheets.
引用
收藏
页码:347 / 354
页数:8
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