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Intermediate Filament Structure
David A.D. Parry,Peter M. Steinert +1 more
- 01 Nov 1994
286
TL;DR: The coiled-coil structure of a rod domain has been elucidated; the basis of the chain interaction and its role in intermediate filament assembly has been specified; the organization of nearest-neighbour molecules in keratin intermediate filaments has been determined; and the glycine loop structures of the terminal domains of epidermal keratin chains have been defined.
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Abstract: In the past year, several new developments concerning the structure of intermediate filament proteins and their assembly into intact intermediate filaments have been made: the coiled-coil structure of a rod domain has been elucidated; the basis of the chain interaction and its role in intermediate filament assembly has been specified; the organization of nearest-neighbour molecules in keratin intermediate filaments has been determined; and the glycine loop structures of the terminal domains of epidermal keratin chains have been defined. In addition, mutations in intermediate filament chains that promote pathology have been reported for the first time.
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Impaired mechanical stability, migration and contractile capacity in vimentin-deficient fibroblasts
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References
The packing of α-helices: simple coiled-coils
TL;DR: In this paper, the two-strand rope and three-stranded rope models were described and used to illustrate the diffraction theory already developed, and it was shown that they would give a diffuse pattern.
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.
TL;DR: The crystal structure of the GCN4Leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
1.5K
Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: Genetic and functional analyses
Pierre A. Coulombe,M. Elizabeth Hutton,Anthony Letal,Adelaide A. Hebert,Amy S. Paller,Elaine Fuchs +5 more
TL;DR: It is demonstrated that two patients with spontaneous cases of Dowling-Meara EBS have point mutations in a critical region in one (K14) of two basal keratin genes, suggesting that the basis for the phenotype in this patient resides in this point mutation.
655
Pair formation and promiscuity of cytokeratins: formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides.
TL;DR: The results show that cytokeratin complex and IF formation in vitro requires the pairing of one representative of each the type I and type II subfamilies into the heterotypic tetramer but that there is no structural incompatibility between any of the members of the two subfam families.
Elucidating the early stages of keratin filament assembly.
Pierre A. Coulombe,Elaine Fuchs +1 more
TL;DR: It is shown that remarkably, these keratins behave as 1:1 complexes even in 9 M urea and in the presence of a reducing agent, suggesting that there may not be a serial sequence of events leading to the assembly of keratin intermediate filaments, but rather a number of associations may take place in parallel.