메뉴 건너뛰기




Volumn 346, Issue 5, 2005, Pages 1393-1407

Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: The unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations

Author keywords

Copper; Nickel; NMR; Prion protein; Structure

Indexed keywords

AMIDE; COPPER; HISTIDINE DERIVATIVE; IMIDAZOLE; NICKEL; NITROGEN; PRION PROTEIN; PROTEIN DERIVATIVE; HISTIDINE; PLACENTA PROTEIN; PLFR PROTEIN, MOUSE; RECOMBINANT PROTEIN;

EID: 13844299350     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.043     Document Type: Article
Times cited : (147)

References (65)
  • 1
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • S.B. Prusiner Prion diseases and the BSE crisis Science 278 1997 245 251
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 2
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations - Protein misfolding in prion disease
    • A.L. Horwich, and J.S. Weissman Deadly conformations - protein misfolding in prion disease Cell 89 1997 499 510
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 5
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • T.L. James, H. Liu, N.B. Ulyanov, S. Farr-Jones, H. Zhang, and D.G. Donne Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform Proc. Natl Acad. Sci. USA 94 1997 10086 10091
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10086-10091
    • James, T.L.1    Liu, H.2    Ulyanov, N.B.3    Farr-Jones, S.4    Zhang, H.5    Donne, D.G.6
  • 6
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
    • D.G. Donne, J.H. Viles, D. Groth, I. Mehlhorn, T.L. James, and F.E. Cohen Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible Proc. Natl Acad. Sci. USA 94 1997 13452 13457
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3    Mehlhorn, I.4    James, T.L.5    Cohen, F.E.6
  • 9
  • 10
    • 0037470178 scopus 로고    scopus 로고
    • Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: Insights from circular dichroism
    • A.P. Garnett, and J.H. Viles Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism J. Biol. Chem. 278 2003 6795 6802
    • (2003) J. Biol. Chem. , vol.278 , pp. 6795-6802
    • Garnett, A.P.1    Viles, J.H.2
  • 12
    • 0033695126 scopus 로고    scopus 로고
    • Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice
    • E. Flechsig, D. Shmerling, I. Hegyi, A.J. Raeber, M. Fischer, and A. Cozzio Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice Neuron 27 2000 399 408
    • (2000) Neuron , vol.27 , pp. 399-408
    • Flechsig, E.1    Shmerling, D.2    Hegyi, I.3    Raeber, A.J.4    Fischer, M.5    Cozzio, A.6
  • 14
    • 3542999252 scopus 로고    scopus 로고
    • 2+ coordination by His96 and His111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein
    • 2+ coordination by His96 and His111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein J. Biol. Chem. 279 2004 32018 32027
    • (2004) J. Biol. Chem. , vol.279 , pp. 32018-32027
    • Jones, C.E.1    Abdelraheim, S.R.2    Brown, D.R.3    Viles, J.H.4
  • 17
    • 0035902869 scopus 로고    scopus 로고
    • XAFS study of the high-affinity copper-binding site of human PrP91-231 and its low-resolution structure in solution
    • S.S. Hasnain, L.M. Murphy, R.W. Strange, J.G. Grossmann, A.R. Clarke, G.S. Jackson, and J. Collinge XAFS study of the high-affinity copper-binding site of human PrP91-231 and its low-resolution structure in solution J. Mol. Biol. 311 2001 467 473
    • (2001) J. Mol. Biol. , vol.311 , pp. 467-473
    • Hasnain, S.S.1    Murphy, L.M.2    Strange, R.W.3    Grossmann, J.G.4    Clarke, A.R.5    Jackson, G.S.6    Collinge, J.7
  • 19
  • 20
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • M. Fischer, T. Rulicke, A. Raeber, A. Sailer, M. Moser, and B. Oesch Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie EMBO J. 15 1996 1255 1264
    • (1996) EMBO J. , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6
  • 21
    • 0030811015 scopus 로고    scopus 로고
    • Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix
    • T. Muramoto, S.J. DeArmond, M. Scott, G.C. Telling, F.E. Cohen, and S.B. Prusiner Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix Nature Med. 3 1997 750 755
    • (1997) Nature Med. , vol.3 , pp. 750-755
    • Muramoto, T.1    Dearmond, S.J.2    Scott, M.3    Telling, G.C.4    Cohen, F.E.5    Prusiner, S.B.6
  • 22
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • D.R. Brown, B. Schmidt, and H.A. Kretzschmar Role of microglia and host prion protein in neurotoxicity of a prion protein fragment Nature 380 1996 345 347
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 23
    • 0027367506 scopus 로고
    • Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro
    • F. Tagliavini, F. Prelli, L. Verga, G. Giaccone, R. Sarma, and P. Gorevic Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro Proc. Natl Acad. Sci. USA 90 1993 9678 9682
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9678-9682
    • Tagliavini, F.1    Prelli, F.2    Verga, L.3    Giaccone, G.4    Sarma, R.5    Gorevic, P.6
  • 24
    • 0035815738 scopus 로고    scopus 로고
    • Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform
    • E. Quaglio, R. Chiesa, and D.A. Harris Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform J. Biol. Chem. 276 2001 11432 11438
    • (2001) J. Biol. Chem. , vol.276 , pp. 11432-11438
    • Quaglio, E.1    Chiesa, R.2    Harris, D.A.3
  • 25
    • 0034705438 scopus 로고    scopus 로고
    • Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • K. Qin, D.S. Yang, Y. Yang, M.A. Chishti, L.J. Meng, and H.A. Kretzschmar Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation J. Biol. Chem. 275 2000 19121 19131
    • (2000) J. Biol. Chem. , vol.275 , pp. 19121-19131
    • Qin, K.1    Yang, D.S.2    Yang, Y.3    Chishti, M.A.4    Meng, L.J.5    Kretzschmar, H.A.6
  • 27
    • 0037380980 scopus 로고    scopus 로고
    • Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic
    • T. Florio, D. Paludi, V. Villa, D.R. Principe, A. Corsaro, and E. Millo Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic J. Neurochem. 85 2003 62 72
    • (2003) J. Neurochem. , vol.85 , pp. 62-72
    • Florio, T.1    Paludi, D.2    Villa, V.3    Principe, D.R.4    Corsaro, A.5    Millo, E.6
  • 28
    • 0035838471 scopus 로고    scopus 로고
    • Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126
    • M.F. Jobling, X. Huang, L.R. Stewart, K.J. Barnham, C. Curtain, and I. Volitakis Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126 Biochemistry 40 2001 8073 8084
    • (2001) Biochemistry , vol.40 , pp. 8073-8084
    • Jobling, M.F.1    Huang, X.2    Stewart, L.R.3    Barnham, K.J.4    Curtain, C.5    Volitakis, I.6
  • 29
    • 0034810585 scopus 로고    scopus 로고
    • Aberrant metal binding by prion protein in human prion disease
    • B.S. Wong, S.G. Chen, M. Colucci, Z. Xie, T. Pan, and T. Liu Aberrant metal binding by prion protein in human prion disease J. Neurochem. 78 2001 1400 1408
    • (2001) J. Neurochem. , vol.78 , pp. 1400-1408
    • Wong, B.S.1    Chen, S.G.2    Colucci, M.3    Xie, Z.4    Pan, T.5    Liu, T.6
  • 30
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • A.M. Thackray, R. Knight, S.J. Haswell, R. Bujdoso, and D.R. Brown Metal imbalance and compromised antioxidant function are early changes in prion disease Biochem. J. 362 2002 253 258
    • (2002) Biochem. J. , vol.362 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 33
    • 0034673578 scopus 로고    scopus 로고
    • The N-terminal tandem repeat region of human prion protein reduces copper: Role of tryptophan residues
    • F.H. Ruiz, E. Silva, and N.C. Inestrosa The N-terminal tandem repeat region of human prion protein reduces copper: role of tryptophan residues Biochem. Biophys. Res. Commun. 269 2000 491 495
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 491-495
    • Ruiz, F.H.1    Silva, E.2    Inestrosa, N.C.3
  • 34
    • 0037160028 scopus 로고    scopus 로고
    • Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron
    • C.J. Maynard, R. Cappai, I. Volitakis, R.A. Cherny, A.R. White, and K. Beyreuther Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron J. Biol. Chem. 277 2002 44670 44676
    • (2002) J. Biol. Chem. , vol.277 , pp. 44670-44676
    • Maynard, C.J.1    Cappai, R.2    Volitakis, I.3    Cherny, R.A.4    White, A.R.5    Beyreuther, K.6
  • 36
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • P.C. Pauly, and D.A. Harris Copper stimulates endocytosis of the prion protein J. Biol. Chem. 273 1998 33107 33110
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 37
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • W.S. Perera, and N.M. Hooper Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region Curr. Biol. 11 2001 519 523
    • (2001) Curr. Biol. , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 38
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • W. Rachidi, D. Vilette, P. Guiraud, M. Arlotto, J. Riondel, and H. Laude Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery J. Biol. Chem. 278 2003 9064 9072
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6
  • 41
    • 0034614481 scopus 로고    scopus 로고
    • The octapeptide repeat region of prion protein binds Cu(II) in the redox-inactive state
    • N. Shiraishi, Y. Ohta, and M. Nishikimi The octapeptide repeat region of prion protein binds Cu(II) in the redox-inactive state Biochem. Biophys. Res. Commun. 267 2000 398 402
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 398-402
    • Shiraishi, N.1    Ohta, Y.2    Nishikimi, M.3
  • 43
    • 0034709641 scopus 로고    scopus 로고
    • Differential contribution of superoxide dismutase activity by prion protein in vivo
    • B.S. Wong, T. Pan, T. Liu, R. Li, P. Gambetti, and M.S. Sy Differential contribution of superoxide dismutase activity by prion protein in vivo Biochem. Biophys. Res. Commun. 273 2000 136 139
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 136-139
    • Wong, B.S.1    Pan, T.2    Liu, T.3    Li, R.4    Gambetti, P.5    Sy, M.S.6
  • 44
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • D.R. Brown, and A. Besinger Prion protein expression and superoxide dismutase activity Biochem. J. 224 1998 423 429
    • (1998) Biochem. J. , vol.224 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 46
    • 0035872476 scopus 로고    scopus 로고
    • Copper and prion disease
    • D.R. Brown Copper and prion disease Brain Res. Bull. 55 2001 165 173
    • (2001) Brain Res. Bull. , vol.55 , pp. 165-173
    • Brown, D.R.1
  • 47
    • 0035254585 scopus 로고    scopus 로고
    • Prion and prejudice: Normal protein and the synapse
    • D.R. Brown Prion and prejudice: normal protein and the synapse Trends Neurosci. 24 2001 85 90
    • (2001) Trends Neurosci. , vol.24 , pp. 85-90
    • Brown, D.R.1
  • 48
    • 0036525729 scopus 로고    scopus 로고
    • Metal ions and prion disease
    • S. Lehmann Metal ions and prion disease Curr. Opin. Chem. Biol. 6 2002 187 192
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 187-192
    • Lehmann, S.1
  • 49
    • 0041302374 scopus 로고    scopus 로고
    • Cellular prion protein function in copper homeostasis and redox signalling at the synapse
    • N. Vassallo, and J. Herms Cellular prion protein function in copper homeostasis and redox signalling at the synapse J. Neurochem. 86 2003 538 544
    • (2003) J. Neurochem. , vol.86 , pp. 538-544
    • Vassallo, N.1    Herms, J.2
  • 50
    • 1242316297 scopus 로고    scopus 로고
    • Copper binding in the prion protein
    • G.L. Millhauser Copper binding in the prion protein Accts. Chem. Res. 37 2004 79 85
    • (2004) Accts. Chem. Res. , vol.37 , pp. 79-85
    • Millhauser, G.L.1
  • 52
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • D.R. Brown, F. Hafiz, L.L. Glasssmith, B.S. Wong, I.M. Jones, C. Clive, and S.J. Haswell Consequences of manganese replacement of copper for prion protein function and proteinase resistance EMBO J. 19 2000 1180 1186
    • (2000) EMBO J. , vol.19 , pp. 1180-1186
    • Brown, D.R.1    Hafiz, F.2    Glasssmith, L.L.3    Wong, B.S.4    Jones, I.M.5    Clive, C.6    Haswell, S.J.7
  • 57
    • 0343320717 scopus 로고
    • Coordination properties of the amide bond
    • H. Sigel, and R.B. Martin Coordination properties of the amide bond Chem. Rev. 82 1982 385 426
    • (1982) Chem. Rev. , vol.82 , pp. 385-426
    • Sigel, H.1    Martin, R.B.2
  • 58
    • 0003746617 scopus 로고
    • Geigy Scientific Tables
    • CIBA-GEIG Ltd Basel, Switzerland
    • C.E. Lentner Geigy Scientific Tables Geigy Scientific Tables vol. 3 1984 CIBA-GEIG Ltd Basel, Switzerland
    • (1984) Geigy Scientific Tables , vol.3
    • Lentner, C.E.1
  • 60
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 61
    • 0001909564 scopus 로고    scopus 로고
    • Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy
    • M. Liu, X. Mao, C. Ye, H. Huang, J.K. Nicholson, and J.C. Lindon Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy J. Magn. Reson. 132 1998 125 129
    • (1998) J. Magn. Reson. , vol.132 , pp. 125-129
    • Liu, M.1    Mao, X.2    Ye, C.3    Huang, H.4    Nicholson, J.K.5    Lindon, J.C.6
  • 62
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • J. Jeener, B.H. Meier, P. Bachmann, and R.R. Ernst Investigation of exchange processes by two-dimensional NMR spectroscopy J. Chem. Phys. 71 1979 4546 4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 63
    • 45449123980 scopus 로고
    • Interative schemes for bilinear operators; Application to spin decoupling
    • A.J. Shaka, C.J. Lee, and A. Pines Interative schemes for bilinear operators; application to spin decoupling J. Magn. Reson. 77 1988 274 293
    • (1988) J. Magn. Reson. , vol.77 , pp. 274-293
    • Shaka, A.J.1    Lee, C.J.2    Pines, A.3
  • 64
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • C. Bartels, T.-H. Xia, M. Billeter, M. Guntert, and K. Wuthrich The program XEASY for computer-supported NMR spectral analysis of biological macromolecules J. Biomol. NMR 5 1995 1 10
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Guntert, M.4    Wuthrich, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.