As indicated in the overview section of this PPG, vimentin consists of a central rod domain flanked by nona-helical head and tail domains. The central rod domain reveals a pronounced seven-residue periodicity, (abcdefg)n, in the distribution of apolar residues. Within this repeat, positions a and d are preferentially occupied by small apolar residues like Leu, lie. Met or Val, typical for a so-called coiled-coil structure (1). A coiled coil is formed by two or more a-helices wound around each other in a 'superhelix', and is a widespread structural motif in proteins (2, 3). This common structural motif enables IF proteins to self-assemble into 10-nm filaments in vitro In the absence of any auxiliary proteins or factors. These filaments are rope-like assemblies made from two to six 4.5-nm protofibrils (i.e., containing eight IF polypeptides each) which, in turn, are made of two intertwined 3-nm protofilaments each (4, 5). Although the molecular architecture of the 3-nm protofilament has not yet been precisely defined, it appears to be made from two antiparallel IF dimers, the latter being 2-stranded a-helical coiled-coils (i.e., formed via the central rod domain) of two parallel, in-register IF polypeptides (also see Figure 6).

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
1P01GM096971-01
Application #
8142487
Study Section
Special Emphasis Panel (ZRG1-CB-D (40))
Project Start
2011-06-15
Project End
2016-05-31
Budget Start
2011-06-15
Budget End
2012-05-31
Support Year
1
Fiscal Year
2011
Total Cost
$254,604
Indirect Cost
Name
Northwestern University at Chicago
Department
Type
DUNS #
005436803
City
Chicago
State
IL
Country
United States
Zip Code
60611
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Lin, Ni-Hsuan; Huang, Yu-Shan; Opal, Puneet et al. (2016) The role of gigaxonin in the degradation of the glial-specific intermediate filament protein GFAP. Mol Biol Cell 27:3980-3990

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