A comprehensive structural analysis of the complete and unmodified Sup35 prion domain in two distinct infectious conformations is presented. A variety of techniques is used to provide structural details of these two prion conformations, one weakly and one strongly propagating strain. The data show that the fibril conformation of both strains share a common amyloid-like core, comprising the glutamine/asparagine rich first 40 residues.
In the weaker strain this stable structure is dramatically expanded to 70 amino acids.
- Brandon H. Toyama
- Mark J. S. Kelly
- Jonathan S. Weissman
