Three-dimensional structures of prion proteins.

Publisher Summary The prevalence of identical global architectures for the proteins implies that conformational transitions between the ubiquitous cellular form and the transmissible spongiform encephalophathies (TSE)-related scrapie form should follow the same pathway for all species. In this chapter, the much-discussed species barrier for infectious transmission of prion diseases is placed in context with subtle local structure variations in this preserved scaffold. However, as present knowledge of structure-function correlations in prion proteins consists primarily of the observation, that the same polypeptide chain can be found either in PrP C or PrP Sc , and neither typical protein functions nor possible functional sites have been unambiguosly identified for PrP C , searches for physiologically relevant structural features have so far been highly speculative.

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