Related ArticlesNMR structure of the mouse prion protein domain PrP(121-321).
Nature. 1996 Jul 11;382(6587):180-2
Authors: Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K
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.
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
J Mol Biol. 2011 Aug 4;
Authors: Biljan I, Ilc G, Giachin G, Raspadori A, Zhukov I, Plavec J, Legname G
The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP(C)) into a misfolded, pathogenic isoform (PrP(Sc)). Spontaneous generation...
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The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
Biochemistry. 2011 Jul 29;
Authors: Julien O, Chatterjee S, Bjorndahl TC, Sweeting B, Acharya S, Semenchenko V, Chakrabartty A, Pai EF, Wishart DS, Sykes BD, Cashman NR
The residue specific urea-induced unfolding patterns of recombinant...
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[NMR paper] Prion protein NMR structures of elk and of mouse/elk hybrids.
Prion protein NMR structures of elk and of mouse/elk hybrids.
Prion protein NMR structures of elk and of mouse/elk hybrids.
Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):646-50
Authors: Gossert AD, Bonjour S, Lysek DA, Fiorito F, Wüthrich K
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...
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[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Biochemistry. 2004 Aug 17;43(32):10393-9
Authors: Lysek DA, Wüthrich K
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified,...
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[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Related Articles Influence of pH on NMR structure and stability of the human prion protein globular domain.
J Biol Chem. 2003 Sep 12;278(37):35592-6
Authors: Calzolai L, Zahn R
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
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[NMR paper] NMR structure of the bovine prion protein.
NMR structure of the bovine prion protein.
NMR structure of the bovine prion protein.
Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8334-9
Authors: López Garcia F, Zahn R, Riek R, Wüthrich K
The NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230), include a globular domain extending from residue 125 to residue 227, a short flexible chain end of residues 228-230, and an N-terminal flexibly disordered "tail" comprising 108 residues for the...
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[NMR paper] The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reve
The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle.
Related Articles The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle.
Biochemistry. 2000 Feb 22;39(7):1604-12
Authors: Klein DJ, Johnson PE, Zollars ES, De Guzman RN, Summers MF
The nucleocapsid protein (NC) from the mouse mammary tumor virus (MMTV) has been overexpressed in Escherichia coli and purified to homogeneity for...
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[NMR paper] Prion protein NMR structure and species barrier for prion diseases.
Prion protein NMR structure and species barrier for prion diseases.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Prion protein NMR structure and species barrier for prion diseases.
Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7281-5
Authors: Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, Wüthrich K
The structural...
NMR structure of the mouse prion protein domain PrP(121-321).
Linear Mode
