1ag2
From Proteopedia
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PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE
Overview
The 'protein only' hypothesis states that a modified form of normal prion, protein triggers infectious neurodegenerative diseases, such as bovine, spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in, humans. Prion proteins are thought to exist in two different, conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential, for understanding the transition to PrPsc. The nuclear magnetic resonance, (NMR) structure of the autonomously folding PrP domain comprising residues, 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three, alpha-helices. This domain contains most of the point-mutation sites that, have been linked, in human PrP, to the occurrence of familial prion, diseases. The NMR structure shows that these mutations occur within, or, directly adjacent to, regular secondary structures. The presence of a, beta-sheet in PrP(121-231) is in contrast with model predictions of an, all-helical structure of PrPc (ref. 8), and may be important for the, initiation of the transition from PrPc to PrPsc.
About this Structure
1AG2 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
NMR structure of the mouse prion protein domain PrP(121-321)., Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K, Nature. 1996 Jul 11;382(6587):180-2. PMID:8700211
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