Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions

• Published in: Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 20; no. 4; pp. 133 - 135
• Main Authors: Blake, Derek J., Tinsley, Jonathon M., Davies, Kay E., Knight, Alex E., Winder, Stephen J., Kendrick-Jones, John
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.04.1995
• Subjects: Amino Acid Sequence; Animals; Cytoskeletal Proteins - chemistry; Cytoskeletal Proteins - metabolism; Dystrophin - chemistry; Dystrophin - genetics; Dystrophin - metabolism; Humans; Membrane Proteins; Molecular Sequence Data; Muscular Dystrophies - genetics; Muscular Dystrophies - metabolism; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Utrophin
• ISSN: 0968-0004; 1362-4326
• DOI: 10.1016/S0968-0004(00)88986-0

Dystrophin, the protein product of the DMD gene, is a component of the muscle-membrane cytoskeleton. Mutations in the DMD gene result in the allelic myopathies Duchenne and Becker muscular dystrophy (DMD and BMD). The majority of mutations causing DMD and BMD are large intragenic deletions. The spectrum of these deletions can be used to explain the differences in the clinical severity between DMD and BMD patients. In general, mutations causing BMD, the milder disorder, maintain the translational reading frame of dystrophin and result in near normal amounts of an internally truncated protein. By contrast, deletions causing DMD disrupt the reading frame of dystrophin, often resulting in premature translational termination. Thus, DMD patients often produce little or no detectable dystrophin. On the basis of sequence and function, dystrophin can be divided into four regions. An amino-terminal actin-binding domain is separated from the cysteine-rich and carboxy-terminal domains by a long rod domain.