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• W2029019715 abstract "Background: Recent studies have identified the human copper chaperone CCS as the presumed factor responsible for copper incorporation into superoxide dismutase (SOD). A lack of knowledge of the chaperone's three-dimensional structure has prevented understanding of how the copper might be transferred.Results: The three-dimensional structure of CCS was homology modelled using the periplasmic protein from the bacterial mercury-detoxification system and the structure of one subunit of the human SOD dimeric enzyme as templates. On the basis of the three-dimensional model, a mechanism for the transfer of copper from CCS to SOD is proposed that accounts for electrostatic acceptor recognition, copper storage and copper-transfer properties.Conclusions: The proposed model identifies a path for copper transfer based on the presence of different metal sites characterized by sulphur ligands. Such a model permits the development of strategies able to interfere with copper incorporation in SOD, providing a possible way to prevent or arrest degeneration in the fatal motor neuron disorder amyotrophic lateral sclerosis." @default.
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• W2029019715 date "1999-08-01" @default.
• W2029019715 modified "2023-10-02" @default.
• W2029019715 title "A model for the incorporation of metal from the copper chaperone CCS into Cu,Zn superoxide dismutase" @default.
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• W2029019715 doi "https://doi.org/10.1016/s0969-2126(99)80117-8" @default.
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