Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae.
Bousset, L., Belrhali, H., Janin, J., Melki, R., Morera, S.(2001) Structure 9: 39-46
- PubMed: 11342133 
- DOI: https://doi.org/10.1016/s0969-2126(00)00553-0
- Primary Citation of Related Structures:  
1G6W, 1G6Y - PubMed Abstract: 
The [URE3] non-Mendelian element of the yeast S. cerevisiae is due to the propagation of a transmissible form of the protein Ure2. The infectivity of Ure2p is thought to originate from a conformational change of the normal form of the prion protein. This conformational change generates a form of Ure2p that assembles into amyloid fibrils. Hence, knowledge of the three-dimensional structure of prion proteins such as Ure2p should help in understanding the mechanism of amyloid formation associated with a number of neurodegenerative diseases.
Organizational Affiliation: 
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.