期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 16, 期 6, 页码 598-605出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1617
关键词
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资金
- Alzheimer's Association [NIRG-08-90967]
- US National Institutes of Health [GM25874]
- Howard Hughes Medical Institute
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM025874, R01GM025874] Funding Source: NIH RePORTER
Prions are proteins that can access multiple conformations, at least one of which is beta-sheet rich, infectious and self-perpetuating in nature. These infectious proteins show several remarkable biological activities, including the ability to form multiple infectious prion conformations, also known as strains or variants, encoding unique biological phenotypes, and to establish and overcome prion species (transmission) barriers. In this Perspective, we highlight recent studies of the yeast prion [PSI+], using various biochemical and structural methods, that have begun to illuminate the molecular mechanisms by which self-perpetuating prions encipher such biological activities. We also discuss several aspects of prion conformational change and structure that remain either unknown or controversial, and we propose approaches to accelerate the understanding of these enigmatic, infectious conformers.
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