Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1.

@article{Banci2007MetalationOT,
  title={Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1.},
  author={Lucia Banci and Ivano Bertini and Nicola D'Amelio and Elisa Libralesso and Paola Turano and Joan Selverstone Valentine},
  journal={Biochemistry},
  year={2007},
  volume={46 35},
  pages={9953-62}
}
The G37R copper-zinc superoxide dismutase (SOD1) is one of the many mutant SOD1 proteins known to cause familial amyotrophic lateral sclerosis by an unknown mechanism. This particular mutation occurs in the beta barrel plug, a region proposed to be critical for the structural stability of the protein. The behavior of G37R asSOD1 was studied in solution where it was observed that, when the protein is fully metalated, its global structure, mobility, and stability are virtually indistinguishable… CONTINUE READING