Creutzfeldt-Jakob disease is due to a mutation causing the misfolding of

The transmissible spongiform encephalopathies or prion diseases are fatal neurodegenerative diseases characterized by spongiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells.They include Creutzfeldt-Jakob disease in humans, scrapie in sheep, and bovine spongiform encephalopathy (mad cow disease) in cattle. It is recognized that prion diseases are protein conformation diseases transmitted by altering the conformation, and hence the physical propeies, of proteins endogenous to the host. Human prion-related protein (PrP), a glycoprotein encoded on the sho arm of chromosome 20, normally is monomeric and rich in a helix. Pathologic prion proteins serve as the templates for the conformational transformation of normal PrP, known as PrPc, into PrPsc. Since one pathologic prion or prion-related protein can serve as a template for the conformational transformation of many times its number of PrPc molecules, prion diseases can be transmitted by the protein alone without the involvement of DNA or RNA.Reference: Explanation: Harper's Biochemistry; 30th edition; Chapter 5; proteins: higher Orders of Structure