A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction.

@article{Amann1998ACO,
  title={A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction.},
  author={Kurt J. Amann and B A Renley and James M. Ervasti},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 43},
  pages={28419-23}
}
The dystrophin rod domain is composed of 24 spectrin-like repeats and was thought to act mainly as a flexible spacer between the amino-terminal actin binding domain and carboxyl-terminal membrane-associated domains. We previously demonstrated that a fragment of the dystrophin rod domain also binds F-actin. However, the nature and extent of rod domain association with F-actin is presently unclear. To begin addressing these questions, we characterized two recombinant proteins representing… CONTINUE READING

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Actin Binding by Basic Spectrin-like Repeats

D. J. Blake, J. M. Tinsley, K. E. Davies
J. Biol • 1996

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