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- W1978585427 abstract "The prion protein displays a unique structural ambiguity in that it can adopt multiple stable conformations under physiological conditions. In our view, this puzzling feature resulted from a sudden environmental change in evolution when the prion, previously an integral membrane protein, got expelled into the extracellular space. Analysis of known vertebrate prions unveils a primordial transmembrane protein encrypted in their sequence, underlying this relocalization hypothesis. Apparently, the time elapsed since this event was insufficient to create a minimally frustrated sequence in the new milieu, probably due to the functional constraints set by the importance of the very flexibility that was created in the relocalization. This scenario may explain why, in a structural sense, the prion protein is still en route toward becoming a foldable globular protein." @default.
- W1978585427 created "2016-06-24" @default.
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- W1978585427 date "2001-04-03" @default.
- W1978585427 modified "2023-10-18" @default.
- W1978585427 title "Prion protein: Evolution caught en route" @default.
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- W1978585427 doi "https://doi.org/10.1073/pnas.071308398" @default.
- W1978585427 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/31852" @default.
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