Dynamics of dystrophin’s actin-binding domain

We have used pulsed EPR, calorimetry, and molecular dynamics simulations to examine the structural mechanism of binding for dystrophin's N-terminal actin-binding domain (ABD1) and compare it to utrophin's ABD1. Like other members of the spectrin superfamily, dystrophin's ABD1 consists of two calponin-homology domains, CH1 and CH2. Several mutations within dystrophin's ABD1 are associated with development of severe degenerative muscle disorders Duchenne and Becker muscular dystrophies, highlighting the importance of understanding its structural biology.

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