Journal Article

FZJ-2012-00920

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dominant-negative effects in prion diseases: insights from molecular dynamics simulations on mouse prion protein chimeras

Cong, X. ; Bongarzone, S. ; Giachin, G. ; Rossetti, G. (Corresponding author)FZJ* ; Carloni, P.FZJ* ; Legname, G.

2013
Taylor & Francis Abingdon, Oxon

This record in other databases:      

Please use a persistent id in citations: doi:10.1080/07391102.2012.712477

Abstract: Mutations in the prion protein (PrP) can cause spontaneous prion diseases in humans (Hu) and animals. In transgenic mice, mutations can determine the susceptibility to the infection of different prion strains. Some of these mutations also show a dominant-negative effect, thus halting the replication process by which wild type mouse (Mo) PrP is converted into Mo scrapie. Using all-atom molecular dynamics (MD) simulations, here we studied the structure of HuPrP, MoPrP, 10 Hu/MoPrP chimeras, and 1 Mo/sheepPrP chimera in explicit solvent. Overall, 2 μs of MD were collected. Our findings suggest that the interactions between α1 helix and N-terminal of α3 helix are critical in prion propagation, whereas the β2–α2 loop conformation plays a role in the dominant-negative effect.

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Contributing Institute(s):

1. Jülich Supercomputing Center (JSC)
2. Computational Biomedicine (IAS-5)

Research Program(s):

1. 411 - Computational Science and Mathematical Methods (POF2-411) (POF2-411)

Appears in the scientific report 2013

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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