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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / chemistry*
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Actins / genetics
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Actins / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Dystrophin / chemistry*
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Dystrophin / genetics
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Dystrophin / metabolism
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Gene Deletion*
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Magnetic Resonance Spectroscopy
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Mice
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Polymerase Chain Reaction
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Structure-Activity Relationship
Substances
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Actins
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Dystrophin
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Peptide Fragments