Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.

@article{Wang2007DiseaseassociatedMA,
  title={Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.},
  author={Jiou Wang and Amy L Caruano-Yzermans and Angela Rodr{\'i}guez and Jonathan P Scheurmann and Hilda H. Slunt and Xiaohang Cao and Jonathan D. Gitlin and P John Hart and David R Borchelt},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 1},
  pages={345-52}
}
A subset of superoxide dismutase 1 (Cu/Zn-SOD1) mutants that cause familial amyotrophic lateral sclerosis (FALS) have heightened reactivity with (-)ONOO and H(2)O(2) in vitro. This reactivity requires a copper ion bound in the active site and is a suggested mechanism of motor neuron injury. However, we have found that transgenic mice that express SOD1-H46R/H48Q, which combines natural FALS mutations at ligands for copper and which is inactive, develop motor neuron disease. Using a direct… CONTINUE READING

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