Copper Has Differential Effect on Prion Protein with Polymorphism of Position 129
| Autor: | B S, Wong, C, Clive, S J, Haswell, R A, Williamson, D R, Burton, P, Gambetti, M S, Sy, I M, Jones, D R, Brown |
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| Rok vydání: | 2000 |
| Předmět: |
Prions
Protein Conformation animal diseases Biophysics chemistry.chemical_element Biochemistry law.invention Superoxide dismutase Mice chemistry.chemical_compound law Valine Animals Humans Molecular Biology Gene Binding Sites Polymorphism Genetic Methionine biology Superoxide Dismutase Circular Dichroism Cell Biology Molecular biology Copper Recombinant Proteins nervous system diseases chemistry Polymorphism (materials science) Recombinant DNA biology.protein Antibody Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 269:726-731 |
| ISSN: | 0006-291X |
| Popis: | The pathology of human prion diseases is affected by polymorphism at amino acid residue 129 of the prion protein gene. Recombinant mouse prion proteins mimicking either form of the polymorphism were prepared to examine their effect on the conformation and the level of superoxide dismutase (SOD) activity of the prion protein. Following the binding of copper atoms to prion protein, antibody mapping and CD analysis detected conformational differences between the two forms of protein. However, neither the level of copper binding nor the level of SOD activity associated with this form of prion protein altered with the identity of codon 129. These results suggest that in the holo-metal binding form of the protein, prion structure but not its SOD activity is affected by polymorphism at codon 129. |
| Databáze: | OpenAIRE |
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