Fragment molecular orbital calculations reveal that the E200K mutation markedly alters local structural stability in the human prion protein

References

• Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363 - 13383
   PubMed Web of Science ®Google Scholar
• Chapman J, Brown P, Rabey JM, Goldfarb LG, Inzelberg R, Gibbs CJ Jr, et al. Transmission of spongiform encephalopathy from a familial Creutzfeldt-Jakob disease patient of Jewish Libyan origin carrying the PRNP codon 200 mutation. Neurology 1992; 42:1249 - 12450
   PubMed Web of Science ®Google Scholar
• Tateishi J. Transmission of human prion diseases to rodents. Seminars in Virology 1996; 7:175 - 180
   Google Scholar
• Govaerts C, Wille H, Prusiner SB, Cohen FE. Prusiner SB. Structural studies of prion proteins Prion Biology and Diseases 2004; 2nd Ed New York Cold Spring Harbor Laboratory Press 243 - 282
   Google Scholar
• Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sönnichsen FD. 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 - 33654
   PubMed Web of Science ®Google Scholar
• Richt JA, Hall SM. BSE case associated with prion protein gene mutation. PLoS Pathog 2008; 4:1000156
   PubMed Web of Science ®Google Scholar
• Ferguson-Smith MA, Richt JA. Rare BSE mutation raises concerns over risks to public health. Nature 2009; 457:1079
   PubMed Web of Science ®Google Scholar
• Nishio M, Umezawa Y, Hirota M, Takeuchi Y. The CH/π interaction: significance in molecular recognition. Tetrahedron 1995; 51:8665 - 8701
   Web of Science ®Google Scholar
• Stites WE. Protein-Protein Interactions: interface structure, binding thermodynamics and mutational analysis. Chem Rev 1997; 97:1233 - 1250
   PubMed Web of Science ®Google Scholar
• Kitaura K, Ikeo E, Asada T, Nakano T, Uebayashi M. Fragment molecular orbital method: An approximate computational method for large molecules. Chem Phys Lett 1999; 313:701 - 706
   Web of Science ®Google Scholar
• Nakano T, Kaminuma T, Sato T, Akiyama Y, Uebayasi M, Kitaura K. Fragment molecular orbital method: Application to polypeptides. Chem Phys Lett 2000; 318:614 - 618
   Web of Science ®Google Scholar
• Fukuzawa K, Kitaura K, Uebayasi M, Nakata K, Kaminuma T, Nakano T. Ab initio quantum mechanical study of the binding energies of human estrogen receptor α with its ligands: An application of fragment molecular orbital method. J Comput Chem 2005; 26:1 - 10
   PubMed Web of Science ®Google Scholar
• Fukuzawa K, Komeiji Y, Mochizuki Y, Kato A, Nakano T, Tanaka S. Intra- and intermolecular interactions between cyclic-AMP receptor protein and DNA: Ab initio fragment molecular orbital study. J Comput Chem 2006; 27:948 - 960
   Google Scholar
• Ito M, Fukuzawa K, Mochizuki Y, Nakano T, Tanaka S. Ab initio fragment molecular orbital study of molecular interactions between liganded retinoid X receptor and its coactivator; Part II: Influence of mutations in transcriptional activation function 2 activating domain core on the molecular interactions. J Phys Chem A 2008; 112:1986 - 1998
   PubMed Web of Science ®Google Scholar
• Ishikawa T, Ishikura T, Kuwata K. Theoretical study of the prion protein based on the fragment molecular orbital method. J Comput Chem 2009; 30:2594 - 2601
   Google Scholar
• MOE version 2008 2008; Montreal, Canada Chemical Computing Group Inc.
   Google Scholar
• Advance/BioStation version 2.0 2008; Tokyo, Japan AdvanceSoft Corporation
   Google Scholar
• Mochizuki Y, Nakano T, Koikegami S, Tanimori S, Abe Y, Nagashima U, et al. A parallelized integral-direct second-order Møller-Plesset perturbation theory method with a fragment molecular orbital scheme. Theor Chem Acc 2004; 112:442 - 452
   Web of Science ®Google Scholar
• Borchelt DR, Taraboulos A, Prusiner SB. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J Biol Chem 1992; 267:16188 - 16199
   PubMed Web of Science ®Google Scholar
• Hornemann S, Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121–231) induced by acidic pH. Proc Natl Acad Sci USA 1998; 95:6010 - 6014
   PubMed Web of Science ®Google Scholar
• Kelly JW. The environmental dependency of protein folding best explains prion and amyloid diseases. Proc Natl Acad Sci USA 1998; 95:930 - 932
   PubMed Web of Science ®Google Scholar
• Kuwata K, Nishida N, Matsumoto T, Kamatari YO, Hosokawa-Muto J, Kodama K, et al. Hot spots in prion protein for pathogenic conversion. Proc Natl Acad Sci USA 2007; 104:11921 - 11926
   PubMed Web of Science ®Google Scholar
• Swietnicki W, Peterson RB, Gambetti P, Surewicz WK. Familial mutation and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 1998; 273:31048 - 31052
   PubMed Web of Science ®Google Scholar
• Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed β-helices into trimers. Proc Natl Acad Sci USA 2004; 101:8342 - 8347
   PubMed Web of Science ®Google Scholar
• Morillas M, Vanik DL, Surewicz WK. On the mechanism of α-helix to β-sheet transition in the recombinant prion protein. Biochemistry 2001; 40:6982 - 6987
   PubMed Web of Science ®Google Scholar