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Deletion analysis of the dystrophin‐actin binding domain
Author(s) -
Corrado K.,
Mills P.L.,
Chamberlain J.S.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00397-1
Subject(s) - dystrophin , actin , binding site , binding domain , peptide sequence , biology , utrophin , consensus sequence , computational biology , sequence (biology) , sequence motif , fusion protein , genetics , chemistry , microbiology and biotechnology , duchenne muscular dystrophy , recombinant dna , gene
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.