Deletion analysis of the dystrophin-actin binding domain

K. Corrado, P. L. Mills, J. S. Chamberlain

Research output: Contribution to journalArticlepeer-review

97 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)255-260
Number of pages6
JournalFEBS Letters
Issue number2-3
StatePublished - May 16 1994
Externally publishedYes


  • Actin binding site
  • Duchenne muscular dystrophy
  • Dystrophin
  • α-Actinin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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