메뉴 건너뛰기




Volumn 272, Issue 2, 1997, Pages 253-265

NMR studies of a viral protein that mimics the regulators of complement activation

Author keywords

Complement; NMR; Protein modules; Short consensus repeats; Sushi domains

Indexed keywords

COMPLEMENT FACTOR H; MATRIX PROTEIN; NITROGEN 13; VIRUS PROTEIN;

EID: 0030870312     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1241     Document Type: Article
Times cited : (110)

References (65)
  • 2
    • 0343050313 scopus 로고
    • A strategy for studying modular proteins: Application to complement modules
    • Barlow P. N., Campbell I. D. A strategy for studying modular proteins: application to complement modules. Nuclear Magnetic Resonance Part C. 1994.
    • (1994) Nuclear Magnetic Resonance Part C
    • Barlow, P.N.1    Campbell, I.D.2
  • 4
    • 0026742163 scopus 로고
    • Solution structure of the fifth repeat of factor H - A second example of the complement control protein module
    • Barlow P. N., Norman D. G., Steinkasserer A., Horne T. J., Pearce J., Sim R. B., Campbell I. D. Solution structure of the fifth repeat of factor H - a second example of the complement control protein module. Biochemistry. 31:1992;3626-3630.
    • (1992) Biochemistry , vol.31 , pp. 3626-3630
    • Barlow, P.N.1    Norman, D.G.2    Steinkasserer, A.3    Horne, T.J.4    Pearce, J.5    Sim, R.B.6    Campbell, I.D.7
  • 6
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T. H., Billeter M., Guntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 6:1995;1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Guntert, P.4    Wüthrich, K.5
  • 7
    • 0028278231 scopus 로고
    • Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses
    • Bergelson J. M., Chan M., Solomon K. R., StJohn N. F., Lin H. M., Finberg R. W. Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses. Proc. Natl Acad. Sci. USA. 91:1994;6245-6248.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6245-6248
    • Bergelson, J.M.1    Chan, M.2    Solomon, K.R.3    Stjohn, N.F.4    Lin, H.M.5    Finberg, R.W.6
  • 8
    • 0030589294 scopus 로고    scopus 로고
    • Identification of a heparin-binding domain in the 7th short consensus repeat of complement factor H-1
    • Blackmore T. K., Sadlon T. A., Ward H. M., Lublin D. M., Gordon D. L. Identification of a heparin-binding domain in the 7th short consensus repeat of complement factor H-1. J. Immunol. 157:1996;5422-5427.
    • (1996) J. Immunol. , vol.157 , pp. 5422-5427
    • Blackmore, T.K.1    Sadlon, T.A.2    Ward, H.M.3    Lublin, D.M.4    Gordon, D.L.5
  • 9
    • 0029063226 scopus 로고
    • Tissue-specific and species-specific expression of SP56, a mouse sperm fertilisation protein
    • Bookbinder L. H., Cheng A., Bleil J. D. Tissue-specific and species-specific expression of SP56, a mouse sperm fertilisation protein. Science. 269:1995;86-89.
    • (1995) Science , vol.269 , pp. 86-89
    • Bookbinder, L.H.1    Cheng, A.2    Bleil, J.D.3
  • 11
    • 0029880767 scopus 로고    scopus 로고
    • Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor
    • Brodbeck W. G., Liu D. C., Sperry J., Mold C., Medof M. E. Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor. J. Immunol. 156:1996;2528-2533.
    • (1996) J. Immunol. , vol.156 , pp. 2528-2533
    • Brodbeck, W.G.1    Liu, D.C.2    Sperry, J.3    Mold, C.4    Medof, M.E.5
  • 15
    • 0028969418 scopus 로고
    • CDNA structure of rabbit C4b-binding protein alpha-chain: Preserved sequence motif in complement regulatory protein modules which bind C4b
    • Defrutos P. G., Dahlback B. cDNA structure of rabbit C4b-binding protein alpha-chain: preserved sequence motif in complement regulatory protein modules which bind C4b. Biochim. Biophys. Acta. 1995;285-289.
    • (1995) Biochim. Biophys. Acta , pp. 285-289
    • Defrutos, P.G.1    Dahlback, B.2
  • 16
    • 0026078308 scopus 로고
    • Epstein-Barr virus complement C3d receptor is an interferon-alpha receptor
    • Delcayre A. X., Salas F., Mathur S., Kovats K., Lotz M., Lernhardt W. Epstein-Barr virus complement C3d receptor is an interferon-alpha receptor. EMBO J. 10:1991;916-926.
    • (1991) EMBO J. , vol.10 , pp. 916-926
    • Delcayre, A.X.1    Salas, F.2    Mathur, S.3    Kovats, K.4    Lotz, M.5    Lernhardt, W.6
  • 17
    • 0026645955 scopus 로고
    • Ultrastructures and interactions of complement factors H and I
    • Di Scippio R. G. Ultrastructures and interactions of complement factors H and I. J. Immunol. 149:1992;2592-2599.
    • (1992) J. Immunol. , vol.149 , pp. 2592-2599
    • Di Scippio, R.G.1
  • 18
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles-virus (Edmonston strain)
    • Dorig R. E., Marcil A., Chopra A., Richardson C. D. The human CD46 molecule is a receptor for measles-virus (Edmonston strain). Cell. 75:1993;295-305.
    • (1993) Cell , vol.75 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 19
    • 0028085953 scopus 로고
    • Analysis of protein-S C4b-binding protein interactions by homology modeling and inhibitory antibodies
    • Fernandez J. A., Villoutreix B. O., Hackeng T. M., Griffin J. H., Bouma B. N. Analysis of protein-S C4b-binding protein interactions by homology modeling and inhibitory antibodies. Biochemistry. 33:1994;11073-11078.
    • (1994) Biochemistry , vol.33 , pp. 11073-11078
    • Fernandez, J.A.1    Villoutreix, B.O.2    Hackeng, T.M.3    Griffin, J.H.4    Bouma, B.N.5
  • 20
    • 0342616123 scopus 로고
    • Spermatogenic cell expression of AM67, a regionally localised protein of the guinea-pig sperm acrosomal matrix
    • Gerton G. L., Maulit M. T., Friday B. B., Winfrey V. P., Olson G. E., Foster J. A. Spermatogenic cell expression of AM67, a regionally localised protein of the guinea-pig sperm acrosomal matrix. Biol. Reproduct. 52:1995.
    • (1995) Biol. Reproduct. , vol.52
    • Gerton, G.L.1    Maulit, M.T.2    Friday, B.B.3    Winfrey, V.P.4    Olson, G.E.5    Foster, J.A.6
  • 23
    • 0029787130 scopus 로고    scopus 로고
    • The 7-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF)
    • Hamann J., Vogel B., Vanschijndel G. M. W., Vanlier R. A. W. The 7-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF). J. Expt. Med. 184:1996;1185-1189.
    • (1996) J. Expt. Med. , vol.184 , pp. 1185-1189
    • Hamann, J.1    Vogel, B.2    Vanschijndel, G.M.W.3    Vanlier, R.A.W.4
  • 24
    • 0029808210 scopus 로고    scopus 로고
    • The amino-terminal module of the C4b-binding protein beta-chain contains the protein S-binding site
    • Hardig Y., Dahlback B. The amino-terminal module of the C4b-binding protein beta-chain contains the protein S-binding site. J. Biol. Chem. 271:1996;20861-20867.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20861-20867
    • Hardig, Y.1    Dahlback, B.2
  • 25
    • 0029889305 scopus 로고    scopus 로고
    • The Epstein-Barr virus-binding site on CD21 is involved in CD23 binding and interleukin-4-induced IgE and IgG4 production by human B-cells
    • Henchozlecoanet S., Jeannin P., Aubry J. P., Graber P., Bradshaw C. G., Pochon S., Bonnefoy J. Y. The Epstein-Barr virus-binding site on CD21 is involved in CD23 binding and interleukin-4-induced IgE and IgG4 production by human B-cells. Immunology. 88:1996;35-39.
    • (1996) Immunology , vol.88 , pp. 35-39
    • Henchozlecoanet, S.1    Jeannin, P.2    Aubry, J.P.3    Graber, P.4    Bradshaw, C.G.5    Pochon, S.6    Bonnefoy, J.Y.7
  • 26
    • 79960698472 scopus 로고
    • Water suppression that works: Excitation sculpting using arbitrary wave-forms and pulsed-field gradients
    • Hwang T. L., Shaka A. J. Water suppression that works: excitation sculpting using arbitrary wave-forms and pulsed-field gradients. J. Magn. Reson. ser. A. 112:1995;175-179.
    • (1995) J. Magn. Reson. Ser. a , vol.112 , pp. 175-179
    • Hwang, T.L.1    Shaka, A.J.2
  • 27
    • 0026544083 scopus 로고
    • Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence
    • Isaacs S. N., Kotwal G. J., Moss B. Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence. Proc. Natl Acad. Sci. USA. 89:1992;628-632.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 628-632
    • Isaacs, S.N.1    Kotwal, G.J.2    Moss, B.3
  • 28
    • 0029037560 scopus 로고
    • Diversity of sites for measles-virus binding and for inactivation of complement C3b and C4b on membrane cofactor protein CD46
    • Iwata K., Seya T., Yanagi Y., Pesando J. M., Johnson P. M., Okabe M., Ueda S., Ariga H., Nagasawa S. Diversity of sites for measles-virus binding and for inactivation of complement C3b and C4b on membrane cofactor protein CD46. J. Biol. Chem. 270:1995;15148-15152.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15148-15152
    • Iwata, K.1    Seya, T.2    Yanagi, Y.3    Pesando, J.M.4    Johnson, P.M.5    Okabe, M.6    Ueda, S.7    Ariga, H.8    Nagasawa, S.9
  • 29
    • 0002442431 scopus 로고    scopus 로고
    • Optimal sampling strategies for the measurement of spin-spin relaxation times
    • Jones J. A., Hogkinson P., Baker A. L., Hore P. J. Optimal sampling strategies for the measurement of spin-spin relaxation times. J. Magn. Reson. ser. B. 113:1996;25-34.
    • (1996) J. Magn. Reson. Ser. B , vol.113 , pp. 25-34
    • Jones, J.A.1    Hogkinson, P.2    Baker, A.L.3    Hore, P.J.4
  • 34
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced single quantum correlation spectroscopy with improved sensitivity
    • Kay L. E., Keiffer P., Saarinen T. Pure absorption gradient enhanced single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keiffer, P.2    Saarinen, T.3
  • 37
    • 0024234820 scopus 로고
    • Identification of distinct C3b and C4b recognition sites in the C3b/C4b receptor (CR1, CD35) by deletion mutagenesis
    • Klickstein L. B., Bartow T. J., Miletic V., Rabson L. D., Smith J. A., Fearon D. T. Identification of distinct C3b and C4b recognition sites in the C3b/C4b receptor (CR1, CD35) by deletion mutagenesis. J. Expt. Med. 168:1988;1699-1717.
    • (1988) J. Expt. Med. , vol.168 , pp. 1699-1717
    • Klickstein, L.B.1    Bartow, T.J.2    Miletic, V.3    Rabson, L.D.4    Smith, J.A.5    Fearon, D.T.6
  • 38
    • 0023718738 scopus 로고
    • Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins
    • Kotwal G. J., Moss B. Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins. Nature. 335:1988;176-178.
    • (1988) Nature , vol.335 , pp. 176-178
    • Kotwal, G.J.1    Moss, B.2
  • 39
    • 0025203480 scopus 로고
    • Inhibition of the complement cascade by the major secretory protein of vaccinia virus
    • Kotwal G. J., Isaacs S. T., McKenzie R., Frank M. M., Moss B. Inhibition of the complement cascade by the major secretory protein of vaccinia virus. Science. 250:1990;827-830.
    • (1990) Science , vol.250 , pp. 827-830
    • Kotwal, G.J.1    Isaacs, S.T.2    McKenzie, R.3    Frank, M.M.4    Moss, B.5
  • 40
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 41
    • 0025761266 scopus 로고
    • Sites within the complement C3b/C4b receptor important for the specificity of ligand binding
    • Krych M., Hourcade D., Atkinson J. P. Sites within the complement C3b/C4b receptor important for the specificity of ligand binding. Proc. Nat. Acad. Sci. USA. 88:1991;4353-4357.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 4353-4357
    • Krych, M.1    Hourcade, D.2    Atkinson, J.P.3
  • 42
    • 0029850245 scopus 로고    scopus 로고
    • Mapping of the domains required for decay acceleration activity of the human factor H-like protein-1 and factor-H
    • Kuhn S., Zipfel P. F. Mapping of the domains required for decay acceleration activity of the human factor H-like protein-1 and factor-H. Eur. J. Immunol. 26:1996;2383-2387.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2383-2387
    • Kuhn, S.1    Zipfel, P.F.2
  • 43
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R. R., Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 44
    • 0024351647 scopus 로고
    • Mapping of the Epsteinn-Barr virus and C3dg binding sites to a common domain on complement receptor type 2
    • Lowell C. A., Klickstein L. B., Carter R. H., Mitchell J. A., Fearon D. T., Ahearn J. M. Mapping of the Epsteinn-Barr virus and C3dg binding sites to a common domain on complement receptor type 2. J. Expt. Med. 170:1989;1931-1943.
    • (1989) J. Expt. Med. , vol.170 , pp. 1931-1943
    • Lowell, C.A.1    Klickstein, L.B.2    Carter, R.H.3    Mitchell, J.A.4    Fearon, D.T.5    Ahearn, J.M.6
  • 45
    • 0028325229 scopus 로고
    • Multiple isoforms of CD46 (membrane cofactor protein) serve as receptors for measles virus
    • Manchester M., Liszewski M. K., Atkinson J. P., Oldstone M. B. A. Multiple isoforms of CD46 (membrane cofactor protein) serve as receptors for measles virus. Proc. Natl Acad. Sci. USA. 91:1994;2161-2165.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2161-2165
    • Manchester, M.1    Liszewski, M.K.2    Atkinson, J.P.3    Oldstone, M.B.A.4
  • 48
    • 0343486172 scopus 로고
    • Improved solvent suppression in one-dimensional and two-dimensional NMR spectra by convolution of time domain data
    • Marion D., Ikura M., Bax A. Improved solvent suppression in one-dimensional and two-dimensional NMR spectra by convolution of time domain data. J. Magn. Reson. 84:1989b;72-84.
    • (1989) J. Magn. Reson. , vol.84 , pp. 72-84
    • Marion, D.1    Ikura, M.2    Bax, A.3
  • 49
    • 0025751635 scopus 로고
    • Determination of the structural basis for selective binding of Epstein-Barr virus D.T to human complement receptor type 2
    • Martin D. R., Kalli K. R., Yuryev A., Fearon D. T., Ahearn J. M. Determination of the structural basis for selective binding of Epstein-Barr virus D.T to human complement receptor type 2. J. Expt. Med. 174:1991;1299-1311.
    • (1991) J. Expt. Med. , vol.174 , pp. 1299-1311
    • Martin, D.R.1    Kalli, K.R.2    Yuryev, A.3    Fearon, D.T.4    Ahearn, J.M.5
  • 50
    • 0028241476 scopus 로고
    • Determination of the role for CD21 during Epstein-Barr virus infection of B lymphoblastoid cells
    • Martin D. R., Marlowe R. L., Ahearn J. M. Determination of the role for CD21 during Epstein-Barr virus infection of B lymphoblastoid cells. J. Virol. 68:1994;4716-4726.
    • (1994) J. Virol. , vol.68 , pp. 4716-4726
    • Martin, D.R.1    Marlowe, R.L.2    Ahearn, J.M.3
  • 52
    • 0024399050 scopus 로고
    • Hydrodynamic, electron microscopic and ligand binding analysis of the Epstein-Barr virus/C3dg receptor (CR2)
    • Moore M. D., Di Scippio R. G., Cooper N. R., Nemarrow G. R. Hydrodynamic, electron microscopic and ligand binding analysis of the Epstein-Barr virus/C3dg receptor (CR2). J. Biol. Chem. 264:1989;20576-20582.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20576-20582
    • Moore, M.D.1    Di Scippio, R.G.2    Cooper, N.R.3    Nemarrow, G.R.4
  • 54
    • 0025894780 scopus 로고
    • The three-dimensional structure of a complement control protein module in solution
    • Norman D. G., Barlow P. N., Baron M., Day A. J., Sim R. B., Campbell I. D. The three-dimensional structure of a complement control protein module in solution. J. Mol. Biol. 219:1991;717-725.
    • (1991) J. Mol. Biol. , vol.219 , pp. 717-725
    • Norman, D.G.1    Barlow, P.N.2    Baron, M.3    Day, A.J.4    Sim, R.B.5    Campbell, I.D.6
  • 55
    • 0028935315 scopus 로고
    • Membrane cofactor protein (CD46) is a keratinocyte receptor for the M-protein of group-A streptococcus
    • Okada N., Liszewski M. K., Atkinson J. P., Caparon M. Membrane cofactor protein (CD46) is a keratinocyte receptor for the M-protein of group-A streptococcus. Proc. Natl Acad. Sci. USA. 92:1995;2489-2493.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2489-2493
    • Okada, N.1    Liszewski, M.K.2    Atkinson, J.P.3    Caparon, M.4
  • 58
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • Reid K. B. M., Day A. J. Structure-function relationships of the complement components. Immunol. Today. 10:1989;177-180.
    • (1989) Immunol. Today , vol.10 , pp. 177-180
    • Reid, K.B.M.1    Day, A.J.2
  • 60
    • 38249028917 scopus 로고
    • Multiple pulse sequences for precise transmitter phase-alignment
    • Shaka A. J., Shykind D. N., Chingas G. C., Pines A. Multiple pulse sequences for precise transmitter phase-alignment. J. Magn. Reson. 80:1988;96-111.
    • (1988) J. Magn. Reson. , vol.80 , pp. 96-111
    • Shaka, A.J.1    Shykind, D.N.2    Chingas, G.C.3    Pines, A.4
  • 61
    • 0029763437 scopus 로고    scopus 로고
    • Identification of 3 physically and functionally distinct binding-sites for C3b in human-complement factor-H by deletion mutagenesis
    • Sharma A. K., Pangburn M. K. Identification of 3 physically and functionally distinct binding-sites for C3b in human-complement factor-H by deletion mutagenesis. Proc. Natl Acad. Sci. USA. 93:1996;10996-11001.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 65
    • 0028054305 scopus 로고
    • Decay-accelerating factor CD55 is identified as the receptor for echovirus-7 using Celics, a rapid immune-focal cloning method
    • Ward T., Pipkin P. A., Clarkson N. A., Stone D. M., Minor P. D., Almond J. W. Decay-accelerating factor CD55 is identified as the receptor for echovirus-7 using Celics, a rapid immune-focal cloning method. EMBO J. 13:1994;5070-5074.
    • (1994) EMBO J. , vol.13 , pp. 5070-5074
    • Ward, T.1    Pipkin, P.A.2    Clarkson, N.A.3    Stone, D.M.4    Minor, P.D.5    Almond, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.