Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae

Background: The [URE3] non-Mendelian element of the yeast S. cerevisiae is due to the propagation of a transmissible form of the protein Ure2. The inf ectivity of Ure2p is thought to originate from a conformational change of t he 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.