BIOA01H3 Lecture Notes - Lecture 25: Fatal Familial Insomnia, Prnp, Beta Sheet
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BIOA01H3 Full Course Notes
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He said that this was a rotein folding problem. Prion proteins can fold in 2 ways: alpha helix which is desirable and non-disease. (c type: cellular, beta sheet which has disease. (s type; scrappy) Beta sheet can clump together and can recruit other healthy proteins in the clumping. Neuro(cid:374)s do(cid:374)"t like clu(cid:373)pi(cid:374)g, (cid:448)ery difficult to degrade so cells die. Conversion of structure is the basis of disease. This is an exception to the central dogma protein protein. Prpc is normal form, prpsc is the bad form. Contaminated beef is consumed with bad form, when it finds our regular prp it binds to it via protein-protein interactions resulting in a hetero dimer. When it binds it will cause it to misfolded into the bad form accumulating the bad form in neurons causing death of neurons. But (cid:449)ait prpc is encoded by a gene in our genome. Prpc is glycosylated and has a lipid anchor.
