Deletion analysis of the dystrophin-actin binding domain.

@article{Corrado1994DeletionAO,
  title={Deletion analysis of the dystrophin-actin binding domain.},
  author={K Corrado and Patrick L. Mills and J. S. Chamberlain},
  journal={FEBS letters},
  year={1994},
  volume={344 2-3},
  pages={255-60}
}
Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin. 

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PCR Protocols: A Guide to Methods and Applications, (Innis

  • R. Higuchi
  • 1990
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