Structure-function aspects of prion proteins.
Prions diseases are fatal neurodegenerative disorders resulting from conformational changes in the prion protein from the normal cellular form, PrPC, to the infectious scrapie isoform, PrPSc. High resolution structures for PrPC are now available, and biochemical investigations are shedding light on the nature and determinants of the conformational transition. Together, these studies are beginning to provide a framework to describe structure-function relationships of the prion protein.
Daggett
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Department of Medicinal Chemistry, University of Washington, Seattle 98195-7610, USA. daggett@u.washington.edu
D000818:Animals; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D018621:PrPC Proteins / Q000737:chemistry / Q000378:metabolism*; D018620:PrPSc Proteins / Q000737:chemistry / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D013045:Species Specificity; D013329:Structure-Activity Relationship
D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions