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The 2.0 A structure of the second calponin homology domain from the actin- binding region of the dystrophin homologue utrophin.

Utrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin- binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin.[1]


  1. The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. Keep, N.H., Norwood, F.L., Moores, C.A., Winder, S.J., Kendrick-Jones, J. J. Mol. Biol. (1999) [Pubmed]
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