Crystal Structures of Polymorphic Prion Protein β1 Peptides Reveal Variable Steric Zipper Conformations

The pathogenesis of prion diseases is associated with the conformational conversion of normal, predominantly α-helical prion protein (PrPC) into a pathogenic form that is enriched with β-sheets (PrPSc). Several PrPC crystal structures have revealed β1-mediated intermolecular sheets, suggesting that...

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Veröffentlicht in:	Biochemistry (Easton) 2015-06, Vol.54 (23), p.3640-3648
Hauptverfasser:	Yu, Lu, Lee, Seung-Joo, Yee, Vivien C
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Substitution Crystallization Databases, Protein Humans Hydrogen Bonding Models, Molecular Molecular Weight Oligopeptides - chemistry Oligopeptides - genetics Peptide Fragments - chemistry Peptide Fragments - genetics Polymorphism, Genetic Prion Proteins Prions - chemistry Prions - genetics Protein Conformation Stereoisomerism Surface Properties
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