β-sheet constitution of prion proteins

Trends in Biochemical Sciences

Volumn 35, Issue 3, 2010, Pages 129-134

  Ji, Hong Fang ^a   Zhang, Hong Yu ^b  

^a SHANDONG UNIVERSITY OF TECHNOLOGY   (China)

^b HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

2 PYRROLIDIN 1 YL N [4 [4 (2 PYRROLIDIN 1 YLACETYLAMINO)BENZYL]PHENYL]ACETAMIDE; ANTIVIRUS AGENT; GN 8; PRION PROTEIN; TETRACYCLINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIVIRAL ACTIVITY; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CREUTZFELDT JAKOB DISEASE; FATAL FAMILIAL INSOMNIA; GERSTMANN STRAUSSLER SCHEINKER SYNDROME; HUMAN; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PRION DISEASES; PRIONS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

MAMMALIA;

EID: 77649156805     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.12.002     Document Type: Article

References (50)

1. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
2. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U S A 95 (1998) 13363-13383
3. Caughey B., and Chesebro B. Transmissible spongiform encephalopathies and prion protein interconversions. Adv. Virus. Res. 56 (2001) 277-311
4. Aguzzi A., and Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 116 (2004) 313-327
5. Aguzzi A., and Heikenwalder M. Pathogenesis of prion diseases: current status and future outlook. Nat. Rev. Microbiol. 4 (2006) 765-775
6. Pan K.M., et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90 (1993) 10962-10966
7. Lysek D.A., et al. Prion protein NMR structures of cats, dogs, pigs, and sheep. Proc. Natl. Acad. Sci. USA 102 (2005) 640-645
8. Calzolai L., et al. Prion protein NMR structures of chickens, turtles, and frogs. Proc. Natl. Acad. Sci. USA 102 (2005) 651-655
9. Riek R., et al. NMR structure of the mouse prion protein domain PrP(121-231). Nature 382 (1996) 180-182
10. Salmona M., et al. Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126. Biochem. J. 342 (1999) 207-214
11. Zhang Y., et al. Molecular dynamics study of the fibril elongation of the prion protein fragment PrP106-126. J. Theor. Biol. 245 (2007) 238-242
12. Zhang H., et al. Conformational transitions in peptides containing two putative α-helices of the prion protein. J. Mol. Biol. 250 (1995) 514-526
13. Kuwata K., et al. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. USA 100 (2003) 14790-14795
14. Boshuizen R.S., et al. An in vitro screening assay based on synthetic prion protein peptides for identification of fibril-interfering compounds. Anal. Biochem. 333 (2004) 372-380
15. De Gioia L., et al. Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J. Biol. Chem. 269 (1994) 7859-7862
16. Forloni G., et al. Neurotoxicity of a prion protein fragment. Nature 362 (1993) 543-546
17. Barducci A., et al. Misfolding pathways of the prion protein probed by molecular dynamics simulations. Biophys. J. 88 (2005) 1334-1343
18. Nguyen J.T., et al. X-ray diffraction of scrapie prion rods and PrP peptides. J. Mol. Biol. 252 (1995) 412-422
19. Laws D.D., et al. Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration. Proc. Natl Acad. Sci. USA 98 (2001) 11686-11690
20. Salmona M., et al. Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein. J. Biol. Chem. 278 (2003) 48146-48153
21. Tagliavini F., et al. Amyloid fibrils in Gerstmann-Straussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele. Cell 79 (1994) 695-703
22. Calzolai L., and Zahn R. Influence of pH on NMR structure and stability of the human prion protein globular domain. J. Biol. Chem. 278 (2003) 35592-35596
23. DeMarco M.L., and Daggett V. From conversion to aggregation: Protofibril formation of the prion protein. Proc. Natl. Acad. Sci. USA 101 (2004) 2293-2298
24. Wille H., et al. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. USA 99 (2002) 3563-3568
25. Govaerts C., et al. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Acad. Sci. USA 101 (2004) 8342-8347
26. Williamson R.A., et al. Mapping the prion protein using recombinant antibodies. J. Virol. 72 (1998) 9413-9941
27. Muramoto T., et al. Recombinant scrapie-like prion protein of 106 amino acids is soluble. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 15457-15462
28. Baskakov I.V., et al. Self-assembly of recombinant prion protein of 106 residues. Biochemistry 39 (2000) 2792-2804
29. Cobb N.J., et al. Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal α-helical domain. J. Biol. Chem. 283 (2008) 34704-34711
30. Cobb N.J., et al. Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure. Proc. Natl. Acad. Sci. USA 104 (2007) 18946-18951
31. Hosszu L.L.P., et al. Conformational properties of β-PrP. J. Biol. Chem. 284 (2009) 21981-21990
32. Minor D.L., and Kim P.S. Measurement of the β-sheet forming propensities of amino acids. Nature 367 (1994) 660-663
33. Tizzano B., et al. The human prion protein α2 helix: a thermodynamic study of its conformational preferences. Proteins 59 (2005) 72-79
34. Yamaguchi K., et al. Critical region for amyloid fibril formation of mouse prion protein: unusual amyloidogenic properties of the helix 2 peptide. Biochemistry 47 (2008) 13242-13251
35. Medori R., et al. Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. Neurology 42 (1992) 669-670
36. Goldfarb L.G., et al. New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred. Lancet 337 (1991) 425-1425
37. Cervenakova L., et al. Novel PRNP sequence variant associated with familial encephalopathy. Am. J. Med. Genet. 88 (1999) 653-656
38. Kuwata K., et al. Hot spots in prion protein for pathogenic conversion. Proc. Natl. Acad. Sci. USA 104 (2007) 11921-11926
39. Yamamoto N., and Kuwata K. Regulating the conformation of prion protein through ligand binding. J. Phys. Chem. B. 113 (2009) 12853-12856
40. Ronga L., et al. Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments. Proteins 66 (2007) 707-715
41. Forloni G., et al. Prion disease: time for a therapy?. Curr. Med. Chem. Imun. Endoc. Metab. Agents 3 (2003) 185-197
42. Wasmer C., et al. Amyloid fibrils of the HET-s (218-289) prion form a β-solenoid with a triangular hydrophobic core. Science 319 (2008) 1523-1526
43. Choi J.H., et al. Site-directed mutagenesis demonstrates the plasticity of the β helix: implications for the structure of the misfolded prion protein. Structure 17 (2009) 1014-1023
44. Choi J.H., et al. Analysis of the sequence and structural features of the left-handed β-helical fold. Proteins 73 (2008) 150-160
45. Iengar P., et al. Conformational and sequence signatures in β helix proteins. Structure 14 (2006) 529-542
46. Parisi G., et al. Dynactins p25 and p27 are predicted to adopt the LβH fold. FEBS Lett. 562 (2004) 1-4
47. C to form β sheet using NMR structures and sequence alignment. Biophys. J. 83 (2002) 1268-1280
48. Pietropaolo A., et al. Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals. Chem. Phys. Chem. 10 (2009) 1500-1510
49. Barnham K.J., et al. Delineating common molecular mechanisms in Alzheimer's and prion diseases. Trends Biochem. Sci. 31 (2006) 465-472
50. Ji H.F., et al. Why are prion diseases precluded by non-mammals?. Trends Biochem. Sci. 32 (2007) 206-208