Intermediate filament structure: the bottom-up approach

被引：80

作者：

Chernyatina, Anastasia A. ^{[1
]}

Guzenko, Dmytro ^{[1
]}

Strelkov, Sergei V. ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Lab Biocrystallog, Dept Pharmaceut & Pharmacol Sci, Leuven, Belgium

来源：

CURRENT OPINION IN CELL BIOLOGY | 2015年 / 32卷

关键词：

HUMAN LAMIN; MOLECULAR ARCHITECTURE; SECONDARY STRUCTURE; CELL ARCHITECTURE; ATOMIC-STRUCTURE; GLOBULAR TAIL; VIMENTIN; DOMAIN; DIMER; 2B;

D O I：

10.1016/j.ceb.2014.12.007

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Intermediate filaments (IFs) result from a key cytoskeletal protein class in metazoan cells, but currently there is no consensus as to their three-dimensional architecture. IF proteins form elongated dimers based on the coiled-coil structure within their central 'rod' domain. Here we focus on the atomic structure of this elementary dimer, elucidated using Xray crystallography on multiple fragments and electron paramagnetic resonance experiments on spin-labelled vimentin samples. In line with conserved sequence features, the rod of all IF proteins is composed of three coiled-coil segments containing heptad and hendecad repeats and interconnected by linkers. In addition, the next assembly intermediate beyond the dimer, the tetramer, could be modelled. The impact of these structural results towards understanding the assembly mechanism is discussed.

引用

页码：65 / 72

页数：8

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