Three-dimensional structures of the prion protein and its doppel.
This article discussed the implications of the structures of PrP and Dpl--with their unusual folds containing N-terminal flexible tails and C-terminal globular domains--to the physiologic functions of PrPC and Dpl, and investigations of a possible structural basis of familial human TSEs. Further relations between TSEs and the PrP structure would include the species barrier of TSEs (which seems to be associated with species-specific structural characteristics of PrPC [25,39,67]), and the conformational transition from PrPC to PrPSc using, for example, molecular dynamic simulations [68,69]. Due to the lack of knowledge on physiologic functions of PrPC, however, and the remaining uncertainty about the exact role of the PrP in TSE pathology, it appears that most or all of the physiologically relevant structure-function correlations of PrPC have yet to be identified.
Riek
Roland
R
Structural Biology Laboratory, Salk Institute, 10010 North Torry Pines Road, La Jolla, CA 92037, USA. riek@sbl.salk.edu
Lührs
Thorsten
T
D000595:Amino Acid Sequence; D000818:Animals; D058851:GPI-Linked Proteins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry*; D017433:Protein Structure, Secondary
D058851:GPI-Linked Proteins; C501125:PRND protein, human; D011328:Prions