Q
a prion disease amino acids change
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Prion diseases, also known as transmissible spongiform encephalopathies, are a group of fatal neurodegenerative disorders. They are caused by the misfolding of the prion protein (PrP) from a normal cellular form (PrPC) to a disease-causing form (PrPSc). This misfolding can be triggered by specific amino acid changes in the PrP gene (PRNP). One well-documented mutation is the substitution of methionine for valine at codon 129, which significantly influences disease susceptibility and phenotype. Other mutations leading to prion disease include insertions, deletions, and point mutations throughout the PRNP gene. These mutations disrupt the normal tertiary structure of the PrP, promoting the misfolded form which is resistant to proteolytic degradation and can aggregate, leading to neuronal damage and the characteristic symptoms of the disease. Understanding these mutations is crucial for diagnosing and developing treatments for prion diseases.
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