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

The protein dystrophin contains a coiled region of amino acids which is treminated by a carboxyl group. This terminal domain may be responsible for dystrophin's function as a binder of neuromuscular and extracellular proteins such as actin, merosin, syntrophin and troglycan. Minor differences exist between proteins that are similar to dystrophin, and all contain the coiled-coil structure that is characterized by a alpha helixes that form six closely bound heptads.