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Curr Opin Cell Biol. 2015 Feb;32:65-72. doi: 10.1016/j.ceb.2014.12.007. Epub 2015 Jan 14.

Intermediate filament structure: the bottom-up approach.

Author information

1
Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium.
2
Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium. Electronic address: sergei.strelkov@pharm.kuleuven.be.

Abstract

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 X-ray 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.

PMID:
25596497
DOI:
10.1016/j.ceb.2014.12.007
[Indexed for MEDLINE]

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