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A Native‐Like Conformation for the C‐Terminal Domain of the Prion Ure2p within its Fibrillar Form
Author(s) -
Habenstein Birgit,
Bousset Luc,
Sourigues Yannick,
Kabani Mehdi,
Loquet Antoine,
Meier Beat H.,
Melki Ronald,
Böckmann Anja
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201202093
Subject(s) - fibril , fungal prion , steric effects , chemistry , crystallography , phenotype , prion protein , domain (mathematical analysis) , yeast , nuclear magnetic resonance spectroscopy , residue (chemistry) , prion proteins , biophysics , saccharomyces cerevisiae , biochemistry , stereochemistry , biology , gene , medicine , mathematical analysis , mathematics , disease , pathology
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.