Local environmental effects on the structure of the prion protein - 01/01/05
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Abstract |
Prion diseases are neurodegenerative diseases causally linked to the partial unfolding and subsequent misfolding and aggregation of the prion protein (PrP). While most proteins fold into a single low energy state, PrP can fold into two distinct isoforms. In its innocuous state, denoted as PrPC, the protein has predominantly α-helical secondary structure, however, PrPC can misfold into an isoform rich in extended structure capable of forming toxic and infectious aggregates. While prion disease is believed to be a protein-only disease, one not requiring any non-protein elements for propagation, the different environments the protein finds itself in vivo likely influence its ability to misfold and aggregate. In this review we will examine various molecules, covalent modifications and environments PrP faces in vivo and the effect they have on PrPʼs local environment and, potentially, conformation. Included in this discussion are: (1) pH, (2) carbohydrates, (3) lipid membranes, (4) metal ions, and (5) small molecules. To cite this article: M.L. DeMarco, V. Daggett, C. R. Biologies 328 (2005).
Le texte complet de cet article est disponible en PDF.Keywords : Prion protein, Protein misfolding, Low pH, Carbohydrates, Membrane, Copper, Molecular dynamics
Plan
Vol 328 - N° 10-11
P. 847-862 - octobre-novembre 2005 Retour au numéroBienvenue sur EM-consulte, la référence des professionnels de santé.
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