The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein

@article{Koenig1988TheCS,
  title={The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein},
  author={M. Koenig and A. P. Monaco and Louis M. Kunkel},
  journal={Cell},
  year={1988},
  volume={53},
  pages={219-228}
}
The complete sequence of the human Duchenne muscular dystrophy (DMD) cDNA has been determined. The 3685 encoded amino acids of the protein product, dystrophin, can be separated into four domains. The 240 amino acid N-terminal domain has been shown to be conserved with the actin-binding domain of alpha-actinin. A large second domain is predicted to be rod-shaped and formed by the succession of 25 triple-helical segments similar to the repeat domains of spectrin. The repeat segment is followed by… CONTINUE READING
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