NR ATXL
AU Ross,E.D.; Minton,A.; Wickner,R.B.
TI Prion domains: sequences, structures and interactions.
QU Nature Cell Biology 2005 Nov; 7(11): 1039-44
PT journal article; review
AB 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.
ZR 100
MH Amyloid/*chemistry; Models, Biological; Molecular Chaperones/*physiology; Prions/*chemistry/classification; Protein Conformation; Protein Structure, Quaternary; *Protein Structure, Tertiary; Repetitive Sequences, Nucleic Acid; Saccharomyces cerevisiae Proteins/chemistry
AD Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA. wickner@helix.nih.gov
SP englisch
PO England