|Cartoon representation - colored by secondary structures|
|Surface representation - colored by chains|
Kinda looks like some sort of monster
Dystrophin's structure is an antiparallel dimer each comprising two calponin homology domains that are linked by a central alpha helix. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane. It is therefore thought to serve as a link from the actin-based cytoskeleton of the muscle cell through the plasma membrane to the extracellular matrix.
Norwood, F. L., A. J. Sutherland-Smith, N. H. Keep, and J. Kendrick-Jones. "The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy." Structure 8.481 (2000). Web. 17 Mar. 2011.
Tinsley, J. M., D. J. Blake, M Pearce, A. E. Knight, and J. Kendrick-Jones. "Dystrophin and related proteins." Current Opinion in Genetic Developement 3.3 June (1993): 484-90. Web. 17 Mar. 2011.
Matsumura, K, and KP Campbell. "Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies." Muscle Verve 17.1 Jan. (1994): 2-15. Web. 17 Mar. 2011.