Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
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چکیده
منابع مشابه
Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.
The prion diseases seem to be caused by a conformational change of the prion protein (PrP) from the benign cellular form PrPC to the infectious scrapie form PrPSc; thus, detailed information about PrP structure may provide essential insights into the mechanism by which these diseases develop. In this study, the secondary structure of the recombinant Syrian hamster PrP of residues 29-231 [PrP(29...
متن کاملSolution structure of Syrian hamster prion protein rPrP(90-231).
NMR has been used to refine the structure of Syrian hamster (SHa) prion protein rPrP(90-231), which is commensurate with the infectious protease-resistant core of the scrapie prion protein PrPSc. The structure of rPrP(90-231), refolded to resemble the normal cellular isoform PrPC spectroscopically and immunologically, has been studied using multidimensional NMR; initial results were published [...
متن کاملCharacterization of recombinant, membrane-attached full-length prion protein.
An abnormal isoform, PrP(Sc), of the normal cellular prion protein (PrP(C)) is the major component of the causative agent of prion diseases. Both isoforms were found to possess the same covalent structures, including a C-terminal glycosylphosphatidylinositol anchor, but different secondary and tertiary structures. In this study, a variant of full-length PrP with an unpaired cysteine at the C te...
متن کاملThe N-terminus of the prion protein is a toxic effector regulated by the C-terminus
PrPC, the cellular isoform of the prion protein, serves to transduce the neurotoxic effects of PrPSc, the infectious isoform, but how this occurs is mysterious. Here, using a combination of electrophysiological, cellular, and biophysical techniques, we show that the flexible, N-terminal domain of PrPC functions as a powerful toxicity-transducing effector whose activity is tightly regulated in c...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1997
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.94.25.13452