Structural organization of brain-derived mammalian prions as probed by hydrogen exchange

One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein, PrP(Sc). We used MS analysis of H/D exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion protein conversion involves refolding of the entire regi...

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Detalles Bibliográficos
Autores principales: Smirnovas, Vytautas, Baron, Gerald S., Offerdahl, Danielle K., Raymond, Gregory J., Caughey, Byron, Surewicz, Witold K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3379881/
https://www.ncbi.nlm.nih.gov/pubmed/21441913
http://dx.doi.org/10.1038/nsmb.2035
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author Smirnovas, Vytautas
Baron, Gerald S.
Offerdahl, Danielle K.
Raymond, Gregory J.
Caughey, Byron
Surewicz, Witold K.
author_facet Smirnovas, Vytautas
Baron, Gerald S.
Offerdahl, Danielle K.
Raymond, Gregory J.
Caughey, Byron
Surewicz, Witold K.
author_sort Smirnovas, Vytautas
collection PubMed
description One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein, PrP(Sc). We used MS analysis of H/D exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion protein conversion involves refolding of the entire region C-terminal to residue ~80–90, and that this region in PrP(Sc) consists of ß-strands and relatively short turns/loops, with no native α-helices present.
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spelling pubmed-33798812012-06-20 Structural organization of brain-derived mammalian prions as probed by hydrogen exchange Smirnovas, Vytautas Baron, Gerald S. Offerdahl, Danielle K. Raymond, Gregory J. Caughey, Byron Surewicz, Witold K. Nat Struct Mol Biol Article One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein, PrP(Sc). We used MS analysis of H/D exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion protein conversion involves refolding of the entire region C-terminal to residue ~80–90, and that this region in PrP(Sc) consists of ß-strands and relatively short turns/loops, with no native α-helices present. 2011-03-27 2011-04 /pmc/articles/PMC3379881/ /pubmed/21441913 http://dx.doi.org/10.1038/nsmb.2035 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Smirnovas, Vytautas
Baron, Gerald S.
Offerdahl, Danielle K.
Raymond, Gregory J.
Caughey, Byron
Surewicz, Witold K.
Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title_full Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title_fullStr Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title_full_unstemmed Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title_short Structural organization of brain-derived mammalian prions as probed by hydrogen exchange
title_sort structural organization of brain-derived mammalian prions as probed by hydrogen exchange
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3379881/
https://www.ncbi.nlm.nih.gov/pubmed/21441913
http://dx.doi.org/10.1038/nsmb.2035
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