1DXX

N-terminal Actin-binding Domain of Human Dystrophin

Summary for 1DXX

• Entry DOI: 10.2210/pdb1dxx/pdb
• Related: 1QAG
• Descriptor: DYSTROPHIN (2 entities in total)
• Functional Keywords: structural protein, dystrophin, muscular dystrophy, calponin homology domain, actin-binding, utrophin
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 4
• Total formula weight: 113837.10

Authors

Norwood, F.L.,Sutherland-Smith, A.J.,Keep, N.H.,Kendrick-Jones, J. (deposition date: 2000-01-20, release date: 2000-05-16, Last modification date: 2023-12-06)

Primary citation

Norwood, F.L.,Sutherland-Smith, A.J.,Keep, N.H.,Kendrick-Jones, J.
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

PubMed Abstract: Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane. Dystrophin 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. Pathogenic mutations in dystrophin result in Duchenne or Becker muscular dystrophy.

PubMed: 10801490
DOI: 10.1016/S0969-2126(00)00132-5

Experimental method

X-RAY DIFFRACTION (2.6 Å)