Identification

Author

Ross ED, Minton A, Wickner RB

Title

Prion Domains: Sequences, structures and interactions

Year

2005

Publication type

Article

Journal

Nature Cell Biology

Created

2015-09-01 14:27:01.255964+00:00

Modified

2016-07-29 22:07:28.266706+00:00

Details

Volume

7

Pages

1039 - 1044

Access

Language

English

URL http://www.nature.com/ncb/journal/v7/n11/full/ncb1105-1039.html
DOI

10.1038/ncb1105-1039

Accessed

2015-09-01

Extended information

Abstract

Mammalian and most fungal infectious proteins (also known as prions) are self-propagating amyloid, a filamentous beta-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 beta-sheet structure.