Atomic structure of vimentin coil 2

Nicolet, Stefan and Herrmann, Harald and Aebi, Ueli and Strelkov, Sergei V.. (2010) Atomic structure of vimentin coil 2. Journal of structural biology, Vol. 170, H. 2. pp. 369-376.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5265310

Downloads: Statistics Overview


Intermediate filaments (IFs) are essential cytoskeletal components in metazoan cells. They assemble from elementary dimers that are built around the central alpha-helical coiled-coil rod domain representing the IF 'signature'. The rod consists of two similarly-sized parts, coil 1 and coil 2, connected by a non-alpha-helical linker L12. Coil 2 is absolutely conserved in length across all IF types and was initially predicted to consist of a short coiled-coil segment 2A based on a heptad pattern of hydrophobic residues, another linker L2 and a coiled-coil segment 2B. Here we present the crystal structure of human vimentin fragment including residues 261-335 i.e. approximately the first half of coil 2. The N-terminal part of this fragment reveals a parallel alpha-helical bundle characterized by 3.5 consecutive hendecad repeats. It is immediately followed by a regular left-handed coiled coil. The distinct non-helical linker L2 is therefore not observed. Together with the previously determined crystal structure of the major part of segment 2B (Strelkov et al., 2001), we can now build a complete atomic model of the 21nm long vimentin coil 2 dimer being a relatively rigid rod.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Aebi)
UniBasel Contributors:Aebi, Ueli
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Academic Press
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:08 Jun 2012 06:48
Deposited On:22 Mar 2012 13:28

Repository Staff Only: item control page