|
|||||
|
|
A Native-Like Conformation for the C-Terminal Domain of the Prion Ure2p within its Fibrillar Form |
|
| Authors: | Habenstein Birgit Bousset Luc Sourigues Yannick Kabani Mehdi Loquet Antoine Meier Beat H Melki Ronald Böckmann Anja |
| Affiliation: | 1. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon?1, 7 passage du Vercors, 69367 Lyon (France);2. Laboratoine d'Enzymologie et Biochimie Structurale, UPR 3082 CNRS, Avenue de la Terrasse, 91198 Gif‐sur‐Yvette (France);3. Physical Chemistry, ETH Zürich, Wolfgang‐Pauli‐Strasse 10, 8093 Zürich (Switzerland) |
| Abstract: | Taking a definite stance: Protein fibrils are often associated with disorder and polymorphism, but the prion fibrils of Ure2p are shown (through solid-state NMR spectroscopy) to be highly ordered, and the conformations of the globular domain to be more restricted within the fibrils (black; see scheme) than in Ure2p single crystals?(red). This finding implies that steric impairment is at the origin of the [URE3] phenotype in yeast. |
| Keywords: | NMR spectroscopy prions protein structures solid‐state NMR spectroscopy Ure2p |
| 本文献已被 PubMed 等数据库收录！ | |