Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil

@article{Wiche1991CloningAS,
  title={Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil},
  author={Gerhard Wiche and Bernd Becker and Kurre T Luber and Georg Weitzer and Maria J. Casta{\~n}{\'o}n and R. Hauptmann and Christian Stratowa and Murray Stewart},
  journal={The Journal of Cell Biology},
  year={1991},
  volume={114},
  pages={83 - 99}
}
We have determined the complete cDNA sequence of rat plectin from a number of well-characterized overlapping lambda gt11 clones. The 4,140-residue predicted amino acid sequence (466,481 D) is consistent with a three-domain structural model in which a long central rod domain, having mainly an alpha-helical coiled coil conformation, is flanked by globular NH2- and COOH-terminal domains. The plectin sequence has a number of repeating motifs. The rod domain has five subregions approximately 200… CONTINUE READING
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