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• W1990322910 startingPage "e1002646" @default.
• W1990322910 abstract "Prion Proteins (PrP) are among a small number of proteins for which large numbers of NMR ensembles have been resolved for sequence mutants and diverse species. Here, we perform a comprehensive principle components analysis (PCA) on the tertiary structures of PrP globular proteins to discern PrP subdomains that exhibit conformational change in response to point mutations and clade-specific evolutionary sequence mutation trends. This is to our knowledge the first such large-scale analysis of multiple NMR ensembles of protein structures, and the first study of its kind for PrPs. We conducted PCA on human (n = 11), mouse (n = 14), and wildtype (n = 21) sets of PrP globular structures, from which we identified five conformationally variable subdomains within PrP. PCA shows that different non-local patterns and rankings of variable subdomains arise for different pathogenic mutants. These subdomains may thus be key areas for initiating PrP conversion during disease. Furthermore, we have observed the conformational clustering of divergent TSE-non-susceptible species pairs; these non-phylogenetic clusterings indicate structural solutions towards TSE resistance that do not necessarily coincide with evolutionary divergence. We discuss the novelty of our approach and the importance of PrP subdomains in structural conversion during disease." @default.
• W1990322910 created "2016-06-24" @default.
• W1990322910 creator A5046072860 @default.
• W1990322910 creator A5051233756 @default.
• W1990322910 date "2012-08-09" @default.
• W1990322910 modified "2023-09-27" @default.
• W1990322910 title "The Landscape of the Prion Protein's Structural Response to Mutation Revealed by Principal Component Analysis of Multiple NMR Ensembles" @default.
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• W1990322910 doi "https://doi.org/10.1371/journal.pcbi.1002646" @default.
• W1990322910 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3415401" @default.
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• W1990322910 hasPublicationYear "2012" @default.
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