Three-dimensional structures of the prion protein and its doppel

Clinics in Laboratory Medicine

Volumn 23, Issue 1, 2003, Pages 209-225

  Riek, Roland ^a   Lührs, Thorsten ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; PROTEIN; PROTEIN DOPPEL; UNCLASSIFIED DRUG;

CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; REVIEW; SIMULATION; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION; THREE DIMENSIONAL IMAGING;

EID: 0037368182     PISSN: 02722712     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0272-2712(02)00070-7     Document Type: Review

References (72)

1. Prusiner SB. Prions. Proc Natl Acad Sci USA 1998;95:13363-83.
2. Weissmann C. Molecular biology of transmissible spongiform encephalopathies. FEBS Lett 1996;389:3-11.
3. Brown P, Gajdusek DC. The human spongiform encephalopathies: kuru, Cretuzfeldt-Jakob disease, and the Gerstmann-Sträussler-Scheinker syndrome. Curr Top Microbiol Immunol 1991;171:1-20.
4. Alper T, Cramp WA, Haig DA, et al. Does the agent of scrapie replicate without nucleic acid? Nature 1967;214:764-6.
5. Griffith JS. Self replication and scrapie. Nature 1967;215:1043-4.
6. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982;216: 136-44.
7. Moore RC, Lee IY, Silverman GL, et al. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol 1999;292: 797-817.
8. Lührs T, Riek R, Güntert P, et al. NMR structure of the human doppel protein. J Mol Biol, in press.
9. Mo H, Moore RC, Cohen FE, et al. Two different neurodegenerative diseases caused by proteins with similar structures. Proc Natl Acad Sci USA 2001;98:2352-7.
10. Sakaguchi S, Katamine S, Nishida N, et al. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996;380:528-31.
11. Rossi D, Cozzio A, Flechsig E, et al. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J 2001;20:694-702.
12. Behrens A, Brandner S, Genoud N, et al. Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue doppel. EMBO Rep 2001;2:347-52.
13. Donne DG, Viles JH, Groth D, et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N-terminus is highly flexible. Proc Natl Acad Sci USA 1997;94:13452-7.
14. James TL, Liu H, Ulyanov NB, et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 1997;94:10086-91.
15. López-García F, Zahn R, Riek R, et al. NMR structure of the bovine prion protein. Proc Natl Acad Sci USA 2000;97:8334-9.
16. Riek R, Hornemann S, Wider G, et al. NMR structure of the mouse prion protein domain PrP(121-231) Nature 1996;382:180-2.
17. Riek R, Hornemann S, Wider G, et al. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 1997;413:282-8.
18. Riek R, Wider G, Billeter M, et al. Prion protein NMR structure and familial human-transmissible spongiform encephalopathies. Proc Natl Acad Sci USA 1998;95: 11667-72.
19. Wüthrich K, Riek R. Three-dimensional structures of prion proteins. Adv Prot Chem 2001;57:55-82.
20. Zahn R, Liu A, Lührs T, et al. NMR solution structure of the human prion protein. Proc Natl Acad Sci USA 2000;97:145-50.
21. Hosszu LL, Baxter NJ, Jackson GS, et al. Structural mobility of the human prion protein probed by backbone hydrogen exchange. Nat Struct Biol 1999;6:740-3.
22. Viles JH, Donne D, Kroon G, et al. Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. Biochemistry 2001;40:2743-53.
23. Schätzl HM, Da Costa M, Taylor L, et al. Prion protein gene variation among primates. J Mol Biol 1995;245:362-74.
24. Wopfner F, Weidenhöfer G, Schneider R, et al. Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 1999; 289:1163-78.
25. Billeter M, Riek R, Wider G, et al. Prion protein NMR structure and species barrier for prion diseases. Proc Natl Acad Sci USA 1997;94:7281-5.
26. Knaus KJ, Morillas M, Swietnicki W, et al. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat Struct Biol 2001;8:770-4.
27. Simonic T, Duga S, Strumbo B, et al. cDNA cloning of turtle prion protein. FEBS Lett 2000;469:33-8.
28. Hegde RS, Mastrianni JA, Scott MR, et al. A transmembrane form of the prion protein in neurodegenerative disease. Science 1998;279:827-34.
29. Hegde RS, Tremblay P, Groth D, et al. Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 1999;402:822-6.
30. Riek R. NMR structure of the mouse prion protein [PhD thesis]. Swiss Federal Institute of Technology, Zurich, Switzerland, ETH Nr. 12759, 1998.
31. Forloni G. Neurotoxicity of beta-amyloid and prion peptides. Curr Opin Neurol 1996; 9:492-500.
32. Zhang Y, Swietnicki W, Zagorski MG, et al. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 2000;275:33650-4.
33. Liu H, Farr-Jones S, Ulyanov NB, et al. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 1999;38:5362-77.
34. Brown DR, Qin K, Herms JW. et al. The cellular prion protein binds copper in vivo. Nature 1998;390:684-7.
35. Stockel J, Safar J, Wallace AC, et al. Prion protein selectively binds copper(II) ions. Biochemistry 1998;37:7185-93.
36. Waggoner DJ, Drisaldi B, Bartnikas TB, et al. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J Biol Chem 2000;275:7455-8.
37. 2+ to the C-terminal domain of the murine prion protein. Biophys J 2001;81:514-25.
38. C directly interacts with proteins involved in signaling pathways. J Biol Chem 2001;276:44604-12.
39. Calzolai L, Lysek DA, Güntert P, et al. NMR structures of three single-residue variants of the human prion protein. Proc Natl Acad Sci USA 2000;97:8340-5.
40. Basler K, Oesch B, Scott M, et al. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 1986;46:417-28.
41. Bazan JF, Fletterick RJ, McKinley MP, et al. Predicted secondary structure and membrane topology of the scrapie prion protein. Prot Eng 1987:1:125-35.
42. Oesch B, Westaway D, Wälchli M, et al. A cellular gene encodes scrapie PrP2730 protein. Cell 1985;40:735-46.
43. Turk E, Teplow DB, Hood LE, et al. Purification and properties of the cellular and scrapie hamster prion proteins. Eur J Biochem 1988;176:21-30.
44. Stahl N, Prusiner SB. Prions and prion proteins. FASEB J 1991;5:2799-807.
45. Rudd PM, Endo T, Colominas C, et al. Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc Natl Acad Sci USA 1999;96:13044-9.
46. Rudd PM, Wormald MR, Wing DR, et al. Prion glycoprotein: structure, dynamics, and roles for the sugars. Biochemistry 2001;40:3759-66.
47. Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem 1991; 266:18217-23.
48. Safar J, Roller PP, Gajdusek DC, et al. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 1993;268:20276-84.
49. Pan KM, Baldwin M, Nguyen J, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993;90:10962-6.
50. Hornemann S, Glockshuber R. Autonomous and reversible folding of a soluble aminoterminally truncated segment of the mouse prion protein. J Mol Biol 1996;262:614-9.
51. Hornemann S, Korth C, Oesch B, et al. Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. FEBS Lett 1997; 413:277-81.
52. Shmerling D, Hegyi I, Fischer M, et al. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 1998;93:203-14.
53. Collinge J, Whittington MA, Sidle KCL, et al. Prion protein is necessary for normal synaptic function. Nature 1994;370:295-7.
54. Tobler I, Gaus SE, Deboer T, et al. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996;380:639-42.
55. Büeler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistent to scrapie. Cell 1993;73:1339-47.
56. Mouillet-Richard S, Ermonval M, Chebassier C, et al. Signal transduction through prion protein. Science 2000;289:1925-8.
57. Gill AC, Ritchie MA, Hunt LG, et al. Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo. EMBO J 2000;19: 5324-31.
58. Manson JC, Clarke AR, McBride PA, et al. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 1994; 3:331-40.
59. Peoc'h K, Manivet P, Blaudny P, et al. Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype. Hum Mutat 2000;15:482.
60. Piccardo P, Dlouhy SR, Lievens PM, et al. Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity. J Neuropathol Exp Neurol 1998;57:979-88.
61. Cohen FE, Pan KM, Huang Z, et al. Structural clues to prion replication. Science 1994; 264:530-1.
62. Billeter M, Wüthrich K. The prion protein globular domain and disease-related mutants studied by molecular dynamics simulations. Arch Virol 2000;16(Suppl):251-63.
63. Wong NK, Renouf DV, Lehmann S, et al. Glycosylation of prions and its effects on protein conformation relevant to amino acid mutations. J Mol Graph Model 2000;18: 126-34, 163-5.
64. Liemann S, Glockshuber R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 1999;38:3258-67.
65. Swietnicki W, Persen RB, Gambetti P, et al. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 1998;273:31048-52.
66. Lehmann S, Harris DA. Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J Biol Chem 1997;272:21479-87.
67. Kaneko K, Zulianello L, Scott M, et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 1997;94:10069-74.
68. Alonso DO, DeArmond SJ, Cohen FE, et al. Mapping the early steps in the pH-induced conformational conversion of the prion protein. Proc Natl Acad Sci USA 2001;98:2985-9.
69. Zuegg J, Gready JE. Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor. Glycobiology 2000;10:959-74.
70. Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-5.
71. Viles JH, Cohen FE, Prusiner SB, et al. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci USA 1999; 96:2042-7.
72. Zhang H, Kaneko K, Nguyen JT, et al. Conformational transitions in peptides containing two putative alpha-helices of the prion protein. J Mol Biol 1995;250:514-26.