1Y15
Mouse Prion Protein with mutation N174T
Summary for 1Y15
| Entry DOI | 10.2210/pdb1y15/pdb |
| Related | 1XYW 1XYX 1Y16 |
| Descriptor | Major prion protein (1 entity in total) |
| Functional Keywords | prp, prion protein, tse, cwd, unknown function |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P04925 |
| Total number of polymer chains | 1 |
| Total formula weight | 13251.75 |
| Authors | Gossert, A.D.,Bonjour, S.,Lysek, D.A.,Fiorito, F.,Wuthrich, K. (deposition date: 2004-11-17, release date: 2004-12-28, Last modification date: 2024-10-09) |
| Primary citation | Gossert, A.D.,Bonjour, S.,Lysek, D.A.,Fiorito, F.,Wuthrich, K. Prion protein NMR structures of elk and of mouse/elk hybrids Proc.Natl.Acad.Sci.Usa, 102:646-650, 2005 Cited by PubMed Abstract: The NMR structure of the recombinant elk prion protein (ePrP), which represents the cellular isoform (ePrPC) in the healthy organism, is described here. As anticipated from the highly conserved amino acid sequence, ePrPC has the same global fold as other mammalian prion proteins (PrPs), with a flexibly disordered "tail" of residues 23-124 and a globular domain 125-226 with three alpha-helices and a short antiparallel beta-sheet. However, ePrPC shows a striking local structure variation when compared with most other mammalian PrPs, in particular human, bovine, and mouse PrPC. A loop of residues 166-175, which links the beta-sheet with the alpha2-helix and is part of a hypothetical "protein X" epitope, is outstandingly well defined, whereas this loop is disordered in the other species. Based on NMR structure determinations of two mouse PrP variants, mPrP[N174T] and mPrP[S170N,N174T], this study shows that the structured loop in ePrPC relates to these two local amino acid exchanges, so that mPrP[S170N,N174T] exactly mimics ePrPC. These results are evaluated in the context of recent reports on chronic wasting disease (CWD) in captive and free-ranging deer and elk in the U.S. and Canada, and an animal model is proposed for support of future research on CWD. PubMed: 15647363DOI: 10.1073/pnas.0409008102 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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