The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins

@article{Hanukoglu1983TheCS,
  title={The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins},
  author={Israel Hanukoglu and Elaine Fuchs},
  journal={Cell},
  year={1983},
  volume={33},
  pages={915-924}
}
We present the cDNA and amino acid sequences of a cytoskeletal keratin from human epidermis (Mr = 56K) that belongs to one of the two classes of keratins (Type I and Type II) present in all vertebrates. In these two types of keratins the central approximately 300 residue long regions share approximately 30% homology both with one another and with the sequences of other IF proteins. Within this region, all IF proteins are predicted to contain four helical domains demarcated from one another by… Expand
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The DNA sequence of a cloned cDNA that is complementary to the mRNA for the 50 kilodalton (kd) human epidermal keratin is determined, providing the first amino acid sequence for a cytoskeletal keratin. Expand
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The evolutionary origins of keratin-like sequences to the genomes of lower eukaryotes are traced, indicating the central role that both types of keratins must play in the assembly and structure of the 8-nm filament. Expand
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The structure of the three-chain unit of the bovine epidermal keratin filament may be viewed as three polypeptide subunits aligned side-by-side with two discrete coiled coil α-helical segments interspersed with regions of non-helix. Expand
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