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 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.
Corrado
K
K
Department of Human Genetics, University of Michigan, Ann Arbor 48109-0618.
Mills
P L
PL
Chamberlain
J S
JS
D000199:Actins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D016189:Dystrophin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017353:Gene Deletion; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D016133:Polymerase Chain Reaction; D013329:Structure-Activity Relationship
D000199:Actins; D016189:Dystrophin; D010446:Peptide Fragments