Structural basis of defects in the sacsin HEPN domain responsible for autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS).

@article{Kozlov2011StructuralBO,
  title={Structural basis of defects in the sacsin HEPN domain responsible for autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS).},
  author={Guennadi Kozlov and Alexey Yu Denisov and Martine Girard and Marie-Jos{\'e}e Dicaire and J. Andrew Hamlin and Peter S McPherson and Bernard Brais and Kalle Gehring},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 23},
  pages={20407-12}
}
Sacsin is a 520-kDa protein mutated in the early-onset neurodevelopmental and neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS). The C terminus of the protein contains an HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain of unknown function. Here, we determined the high-resolution 1.9-Å crystal structure of the HEPN domain from human sacsin. The structure is composed of five parallel α-helices with a large loop of several short helical… CONTINUE READING

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