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- W2031034110 abstract "A C-terminally truncated Y145Stop variant of the human prion protein (huPrP23–144) is associated with a hereditary amyloid disease known as PrP cerebral amyloid angiopathy. Previous studies have shown that recombinant huPrP23–144 can be efficiently converted in vitro to the fibrillar amyloid state, and that residues 138 and 139 play a critical role in the amyloidogenic properties of this protein. Here, we have used magic-angle spinning solid-state NMR spectroscopy to provide high-resolution insight into the protein backbone conformation and dynamics in fibrils formed by 13 C, 15 N-labeled huPrP23–144. Surprisingly, we find that signals from ≈100 residues (i.e., ≈80% of the sequence) are not detected above approximately −20°C in conventional solid-state NMR spectra. Sequential resonance assignments revealed that signals, which are observed, arise exclusively from residues in the region 112–141. These resonances are remarkably narrow, exhibiting average 13 C and 15 N linewidths of ≈0.6 and 1 ppm, respectively. Altogether, the present findings indicate the existence of a compact, highly ordered core of huPrP23–144 amyloid encompassing residues 112–141. Analysis of 13 C secondary chemical shifts identified likely β-strand segments within this core region, including β-strand 130–139 containing critical residues 138 and 139. In contrast to this relatively rigid, β-sheet-rich amyloid core, the remaining residues in huPrP23–144 amyloid fibrils under physiologically relevant conditions are largely unordered, displaying significant conformational dynamics." @default.
- W2031034110 created "2016-06-24" @default.
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- W2031034110 date "2008-04-29" @default.
- W2031034110 modified "2023-10-16" @default.
- W2031034110 title "Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils" @default.
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- W2031034110 doi "https://doi.org/10.1073/pnas.0711716105" @default.
- W2031034110 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2359773" @default.
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