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      • Solution Structure of a Prion Protein: Implications for Infectivity

        He Liu,Shauna Farr-Jones,Nikolai Ulyanov,Manuel Llinas,Susan Marqusee,Fred E. Cohen,Stanley B. Prusiner,Thomas L. James 한국자기공명학회 1998 Journal of the Korean Magnetic Resonance Society Vol.2 No.2

        Prions cause neurodegenerative diseases in animals and humans. The scrapie prion protein (PrPSc) is the major – possibly only – component of the infectious prion and is generated from the cellular isoform (PrPC) by a conformational change. Limited proteolysis of PrPSc produces a polypeptide comprised primarily of residues 90 to 231, which retains infectivity. The three-dimensional structure of rPrP(90-231), a recombinant protein resembling PrPC with the Syrian hamster (SHa) sequence, was solved using multidimensional NMR. Low-resolution structures of rPrP(90-231), synthetic peptides up to 56 residues, a longer (29-231, full-length) protein with SHa sequence, and a shorter (121-231) protein with the mouse sequence have been previously reported. We report here further structure refinement of rPrP(90-231) and dynamic features of the protein. Consideration of these features in the context of published data suggests regions of conformational heterogeneity, structural elements involved in the PrPC  PrPSc transformation, and possible structural features related to a species barrier to transmission of prion diseases 영어논문

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