cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.

@article{Fisher1986cDNASO,
  title={cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.},
  author={Daniel Z. Fisher and Nilika Chaudhary and Gunter Blobel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1986},
  volume={83 17},
  pages={6450-4}
}
The amino acid sequences deduced from cDNA clones of human lamin A and lamin C show identity between these two lamins except for an extra 9.0-kDa carboxyl-terminal tail that is present only in lamin A. Both lamins A and C contain an alpha-helical domain of approximately 360 residues that shows striking homology to a corresponding alpha-helical rod domain that is the structural hallmark of all intermediate filament proteins. However, the lamin alpha-helical domain is 14% larger than that of the… CONTINUE READING
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