Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involve...

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Bibliographic Details
Published in:	Nature structural & molecular biology Vol. 18; no. 4; pp. 504 - 506
Main Authors:	Surewicz, Witold K, Smirnovas, Vytautas, Baron, Gerald S, Offerdahl, Danielle K, Raymond, Gregory J, Caughey, Byron
Format:	Journal Article
Language:	English
Published:	New York Nature Publishing Group US 01-04-2011 Nature Publishing Group
Subjects:	631/1647/2258 631/45/535 692/699/375/365/1937 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Brain Brain Chemistry brief-communication Deuterium Genetic aspects Hydrogen Ion exchange Life Sciences Mammals Mass Spectrometry Membrane Biology Molecular biology Physiological aspects Prion diseases Prions Prions - chemistry Protein Structure Proteins Risk factors Structure United States
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Summary:	One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrPSc consists of β-strands and relatively short turns and/or loops, with no native α-helices present.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1
ISSN:	1545-9993 1545-9985
DOI:	10.1038/nsmb.2035