Access
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
Review
Nature Cell Biology 7, 1039–1044 (1 November 2005) | doi:10.1038/ncb1105-1039
Prion domains: sequences, structures and interactions
&
Abstract
Mammalian and most fungal infectious proteins (also known as prions) are self-propagating amyloid, a filamentous β-sheet structure. A prion domain determines the infectious properties of a protein by forming the core of the amyloid. We compare the properties of known prion domains and their interactions with the remainder of the protein and with chaperones. Ure2p and Sup35p, two yeast prion proteins, can still form prions when the prion domains are shuffled, indicating a parallel in-register β-sheet structure.
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
