Abstract
Dystrophin, the product of the gene mutated in Duchenne muscular dystrophy (DMD) is bound by its C-terminus to a protein complex including the related protein dystrobrevin. Both proteins contain a putative coiled-coil domain consisting of two alpha-helices. It has been reported that the two proteins bind to each other by the first one of the two alpha-helices. We have revisited this question using the Caenorhabditis elegans homologs of dystrophin and dystrobrevin. In vitro interaction occurs through the more conserved second helix. We propose a new model of dystrophin interactions with associated proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Caenorhabditis elegans / chemistry*
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Caenorhabditis elegans Proteins*
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Dystrophin / chemistry
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Dystrophin / metabolism*
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Dystrophin-Associated Proteins*
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Glutathione Transferase / metabolism
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Humans
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Models, Biological
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Molecular Sequence Data
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Muscle Proteins / chemistry
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Muscle Proteins / metabolism*
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Nerve Tissue Proteins*
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Neuropeptides / chemistry
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Neuropeptides / metabolism*
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Protein Binding
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Protein Conformation
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Caenorhabditis elegans Proteins
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DTNA protein, human
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Dyb-1 protein, C elegans
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Dystrophin
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Dystrophin-Associated Proteins
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Membrane Proteins
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Muscle Proteins
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Nerve Tissue Proteins
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Neuropeptides
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Recombinant Fusion Proteins
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syntrophin
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Glutathione Transferase