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 intact protein and 4 residues for bPrP(121-230), respectively. The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-226, and a short antiparallel beta-sheet comprising the residues 128-131 and 161-164. The best-defined parts of the globular domain are the central portions of the helices 2 and 3, which are linked by the only disulfide bond in bPrP. Significantly increased disorder and mobility is observed for helix 1, the loop 166-172 leading from the beta-strand 2 to helix 2, the end of helix 2 and the following loop, and the last turn of helix 3. Although there are characteristic local differences relative to the conformations of the murine and Syrian hamster prion proteins, the bPrP structure is essentially identical to that of the human prion protein. On the other hand, there are differences between bovine and human PrP in the surface distribution of electrostatic charges, which then appears to be the principal structural feature of the "healthy" PrP form that might affect the stringency of the species barrier for transmission of prion diseases between humans and cattle.
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] NMR structure of the bovine prion protein isolated from healthy calf brains.
NMR structure of the bovine prion protein isolated from healthy calf brains.
Related Articles NMR structure of the bovine prion protein isolated from healthy calf brains.
EMBO Rep. 2004 Dec;5(12):1159-64
Authors: Hornemann S, Schorn C, Wüthrich K
NMR structures of recombinant prion proteins from various species expressed in Escherichia coli have been solved during the past years, but the fundamental question of the relevancy of these data relative to the naturally occurring forms of the prion protein has not been directly addressed. Here, we...
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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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11-24-2010 09:01 PM
[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
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11-19-2010 08:44 PM
[NMR paper] Prion protein NMR structure and familial human spongiform encephalopathies.
Prion protein NMR structure and familial human spongiform encephalopathies.
Related Articles Prion protein NMR structure and familial human spongiform encephalopathies.
Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11667-72
Authors: Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K
The refined NMR structure of the mouse prion protein domain mPrP(121-231) and the recently reported NMR structure of the complete 208-residue polypeptide chain of mPrP are used to investigate the structural basis of inherited human transmissible...
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11-17-2010 11:15 PM
[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...
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08-22-2010 05:08 PM
[NMR paper] NMR structure of the mouse prion protein domain PrP(121-321).
NMR structure of the mouse prion protein domain PrP(121-321).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles NMR 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...
NMR structure of the bovine prion protein.
Linear Mode
