Deletion analysis of the dystrophin‐actin binding domain
- 16 May 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 344 (2-3) , 255-260
- https://doi.org/10.1016/0014-5793(94)00397-1
Abstract
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.Keywords
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