DELETION ANALYSIS OF THE DYSTROPHIN-ACTIN BINDING DOMAIN

Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a ser ies of purified bacterial fusion proteins deleted for each of these si tes we have demonstrated that none of the three are critical for dystr ophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTF T motif, contain the major site for interaction with actin.