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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural plasticity of the cellular prion protein and implications in health and disease
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Structural plasticity of the cellular prion protein and implications in health and disease

机译：Structural plasticity of the cellular prion protein and implications in health and disease

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摘要

Two lines of transgenic mice expressing mouse/elk and mouse/ horse prion protein (PrP) hybrids, which both form a well-structured β2-α2 loop in the NMR structures at 20 °C termed rigid-loop cellular prion proteins (RL-PrP~C), presented with accumulation of the aggregated scrapie form of PrP in brain tissue, and the mouse/ elk hybrid has also been shown to develop a spontaneous transmissible spongiform encephalopathy. Independently, there is in vitro evidence for correlations between the amino acid sequence in the β2-α2 loop and the propensity for conformational transitions to disease-related forms of PrP. To further contribute to the structural basis for these observations, this paper presents a detailed characterization of RL-PrP~C conformations in solution. A dynamic local conformational polymorphism involving the β2-α2 loop was found to be evolutionarily preserved among all mammalian species, including those species for which the WT PrP forms an RL-PrP~C. The interconversion between two ensembles of PrP~C conformers that contain, respectively, a 3_(10)-helix turn or a type I β-turn structure of the β2-α2 loop, exposes two different surface epitopes, which are analyzed for their possible roles in the still evasive function of PrP~C in healthy organisms and/or at the onset of a transmissible spongiform encephalopathy.

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