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Volumn 356, Issue 2, 2006, Pages 397-412

Extended flexible linker structures in the complement chimaeric conjugate CR2-Ig by scattering, analytical ultracentrifugation and constrained modelling: Implications for function and therapy

Author keywords

Analytical ultracentrifugation; Constrained modelling; Neutron scattering; Short consensus complement repeat; X ray scattering

Indexed keywords

COMPLEMENT COMPONENT C3D; COMPLEMENT COMPONENT C3D RECEPTOR; COMPLEMENT INHIBITOR; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1;

EID: 30744466395     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.050     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 0025971707 scopus 로고
    • Expression of CR2 (the C3d,g/EBV receptor, CD21) on normal human peripheral blood T lymphocytes
    • E. Fischer, C. Delibrias, and M.D. Kazatchkine Expression of CR2 (the C3d,g/EBV receptor, CD21) on normal human peripheral blood T lymphocytes J. Immunol. 146 1991 865 869
    • (1991) J. Immunol. , vol.146 , pp. 865-869
    • Fischer, E.1    Delibrias, C.2    Kazatchkine, M.D.3
  • 3
    • 0026756465 scopus 로고
    • Characterization of an Epstein-Barr virus receptor on human epithelial cells
    • M. Birkenbach, X. Tung, L.E. Bradbury, T.F. Tedder, and E. Kieff Characterization of an Epstein-Barr virus receptor on human epithelial cells J. Expt. Med. 176 1992 1405 1414
    • (1992) J. Expt. Med. , vol.176 , pp. 1405-1414
    • Birkenbach, M.1    Tung, X.2    Bradbury, L.E.3    Tedder, T.F.4    Kieff, E.5
  • 5
    • 0022869958 scopus 로고
    • A re-evaluation of the role of C3 in B-cell activation
    • G.B. Klaus, and J.H. Humphrey A re-evaluation of the role of C3 in B-cell activation Immunol. Today 7 1986 163 165
    • (1986) Immunol. Today , vol.7 , pp. 163-165
    • Klaus, G.B.1    Humphrey, J.H.2
  • 6
    • 0025127325 scopus 로고
    • In vivo inhibition of the antibody response by a complement receptor-specific monoclonal antibody
    • B. Heyman, E.J. Wiersma, and T. Kinoshita In vivo inhibition of the antibody response by a complement receptor-specific monoclonal antibody J. Expt. Med. 172 1990 665 668
    • (1990) J. Expt. Med. , vol.172 , pp. 665-668
    • Heyman, B.1    Wiersma, E.J.2    Kinoshita, T.3
  • 8
    • 0027244776 scopus 로고
    • CD23 and CD21 function as adhesion molecules in homotypic aggregation of human B lymphocytes
    • P. Björck, C. Elenstrom-Magnusson, A. Rosen, E. Severinson, and S. Paulie CD23 and CD21 function as adhesion molecules in homotypic aggregation of human B lymphocytes Eur. J. Immunol. 23 1993 1771 1775
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1771-1775
    • Björck, P.1    Elenstrom-Magnusson, C.2    Rosen, A.3    Severinson, E.4    Paulie, S.5
  • 9
    • 0026480851 scopus 로고
    • T lymphocyte expression of complement receptor 2 (CR2/CD21): A role in adhesive cell-cell interactions and dysregulation in a patient with systemic lupus erythematosus (SLE)
    • E. Levy, J. Ambrus, L. Kahl, H. Molina, K. Tung, and V.M. Holers T lymphocyte expression of complement receptor 2 (CR2/CD21): a role in adhesive cell-cell interactions and dysregulation in a patient with systemic lupus erythematosus (SLE) Clin. Expt. lmmunol. 90 1992 235 244
    • (1992) Clin. Expt. Lmmunol. , vol.90 , pp. 235-244
    • Levy, E.1    Ambrus, J.2    Kahl, L.3    Molina, H.4    Tung, K.5    Holers, V.M.6
  • 11
    • 0028181248 scopus 로고
    • CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21
    • J.-P. Aubry, S. Pochon, J.-F. Gauchat, A. Nueda-Marin, V.M. Holers, and P. Graber CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21 J. Immunol. 152 1994 5806 5813
    • (1994) J. Immunol. , vol.152 , pp. 5806-5813
    • Aubry, J.-P.1    Pochon, S.2    Gauchat, J.-F.3    Nueda-Marin, A.4    Holers, V.M.5    Graber, P.6
  • 12
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d: A C3 fragment and ligand for complement receptor 2
    • B. Nagar, R.G. Jones, R.J. Diefenbach, D.E. Isenman, and J.M. Rini X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2 Science 280 1998 1277 1281
    • (1998) Science , vol.280 , pp. 1277-1281
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 14
    • 0036678090 scopus 로고    scopus 로고
    • The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding
    • A.E. Prota, D.R. Sage, T. Stehle, and J.D. Fingeroth The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding Proc. Natl Acad. Sci. USA 99 2002 10641 10646
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 10641-10646
    • Prota, A.E.1    Sage, D.R.2    Stehle, T.3    Fingeroth, J.D.4
  • 15
    • 0035918584 scopus 로고    scopus 로고
    • Structural studies in solution of the recombinant N-terminal pair of short consensus/complement repeat domains of complement receptor type 2 (CR2/CD21) and its interaction with its ligand C3dg
    • J.M. Guthridge, J.K. Rakstang, K.A. Young, J. Hinshelwood, M. Aslam, and A. Robertson Structural studies in solution of the recombinant N-terminal pair of short consensus/complement repeat domains of complement receptor type 2 (CR2/CD21) and its interaction with its ligand C3dg Biochemistry 40 2001 5931 5941
    • (2001) Biochemistry , vol.40 , pp. 5931-5941
    • Guthridge, J.M.1    Rakstang, J.K.2    Young, K.A.3    Hinshelwood, J.4    Aslam, M.5    Robertson, A.6
  • 16
    • 0034292433 scopus 로고    scopus 로고
    • Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21)
    • L. Clemenza, and D.E. Isenman Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21) J. Immunol. 165 2000 3839 3848
    • (2000) J. Immunol. , vol.165 , pp. 3839-3848
    • Clemenza, L.1    Isenman, D.E.2
  • 17
    • 13844255020 scopus 로고    scopus 로고
    • Mutational analysis of the complement receptor type 2 (CR2/CD21)-C3d interaction reveals a putative charged SCR 1 binding site for C3d
    • J.P. Hannan, K.A. Young, J.M. Guthridge, R. Asokan, G. Szakonyi, X.S. Chen, and V.M. Holers Mutational analysis of the complement receptor type 2 (CR2/CD21)-C3d interaction reveals a putative charged SCR 1 binding site for C3d J. Mol. Biol. 346 2005 845 858
    • (2005) J. Mol. Biol. , vol.346 , pp. 845-858
    • Hannan, J.P.1    Young, K.A.2    Guthridge, J.M.3    Asokan, R.4    Szakonyi, G.5    Chen, X.S.6    Holers, V.M.7
  • 18
    • 13844266308 scopus 로고    scopus 로고
    • Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: An X-ray scattering and sedimentation modelling study
    • H.E. Gilbert, J.T. Eaton, J.P. Hannan, V.M. Holers, and S.J. Perkins Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: an X-ray scattering and sedimentation modelling study J. Mol. Biol. 346 2005 859 873
    • (2005) J. Mol. Biol. , vol.346 , pp. 859-873
    • Gilbert, H.E.1    Eaton, J.T.2    Hannan, J.P.3    Holers, V.M.4    Perkins, S.J.5
  • 19
    • 0024399050 scopus 로고
    • Hydrodynamic, electron microscopic and ligand-binding analysis of the Epstein-Barr virus/C3dg receptor (CR2)
    • M.D. Moore, R.G. DiScipio, N.R. Cooper, and G.R. Nemerow 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    Discipio, R.G.2    Cooper, N.R.3    Nemerow, G.R.4
  • 21
    • 0037954130 scopus 로고    scopus 로고
    • The extended multidomain solution structures of the complement protein Crry and its chimaeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: Implications for function and therapy
    • M. Aslam, J.M. Guthridge, B.K. Hack, R.J. Quigg, V.M. Holers, and S.J. Perkins The extended multidomain solution structures of the complement protein Crry and its chimaeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy J. Mol. Biol. 329 2003 525 550
    • (2003) J. Mol. Biol. , vol.329 , pp. 525-550
    • Aslam, M.1    Guthridge, J.M.2    Hack, B.K.3    Quigg, R.J.4    Holers, V.M.5    Perkins, S.J.6
  • 22
    • 0025991505 scopus 로고
    • Suppression of the immune response by a soluble complement receptor of B lymphocytes
    • T. Hebell, J.M. Ahearn, and D.T. Fearon Suppression of the immune response by a soluble complement receptor of B lymphocytes Science 254 1991 102 105
    • (1991) Science , vol.254 , pp. 102-105
    • Hebell, T.1    Ahearn, J.M.2    Fearon, D.T.3
  • 23
    • 85047692710 scopus 로고    scopus 로고
    • Complement receptor 2-mediated targeting of complement inhibitors to sites of complement activation
    • H. Song, C. He, C. Knaak, J.M. Guthridge, V.M. Holers, and S. Tomlinson Complement receptor 2-mediated targeting of complement inhibitors to sites of complement activation J Clin Invest. 111 2003 1875 1885
    • (2003) J Clin Invest. , vol.111 , pp. 1875-1885
    • Song, H.1    He, C.2    Knaak, C.3    Guthridge, J.M.4    Holers, V.M.5    Tomlinson, S.6
  • 24
    • 77956826381 scopus 로고
    • X-ray and neutron solution scattering
    • S.J. Perkins X-ray and neutron solution scattering New Compr. Biochem. 11B 1988 143 265
    • (1988) New Compr. Biochem. , vol.11 , pp. 143-265
    • Perkins, S.J.1
  • 25
    • 0035933335 scopus 로고    scopus 로고
    • Folded-back solution structure of monomeric Factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
    • M. Aslam, and S.J. Perkins Folded-back solution structure of monomeric Factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling J. Mol. Biol. 309 2001 1117 1138
    • (2001) J. Mol. Biol. , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 26
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: A study by X-ray and neutron solution scattering and homology modelling
    • M.K. Boehm, J.M. Woof, M.A. Kerr, and S.J. Perkins The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling J. Mol. Biol. 286 1999 1421 1447
    • (1999) J. Mol. Biol. , vol.286 , pp. 1421-1447
    • Boehm, M.K.1    Woof, J.M.2    Kerr, M.A.3    Perkins, S.J.4
  • 27
    • 2142643646 scopus 로고    scopus 로고
    • Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: A comparison with monomeric human IgA1
    • P.B. Furtado, P.W. Whitty, A. Robertson, J.T. Eaton, A. Almogren, and M.A. Kerr Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: a comparison with monomeric human IgA1 J. Mol. Biol. 338 2004 921 941
    • (2004) J. Mol. Biol. , vol.338 , pp. 921-941
    • Furtado, P.B.1    Whitty, P.W.2    Robertson, A.3    Eaton, J.T.4    Almogren, A.5    Kerr, M.A.6
  • 28
    • 25144489575 scopus 로고    scopus 로고
    • Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering
    • Z. Sun, A. Almogren, P.B. Furtado, B. Chowdhury, M.A. Kerr, and S.J. Perkins Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering J. Mol. Biol. 353 2005 155 173
    • (2005) J. Mol. Biol. , vol.353 , pp. 155-173
    • Sun, Z.1    Almogren, A.2    Furtado, P.B.3    Chowdhury, B.4    Kerr, M.A.5    Perkins, S.J.6
  • 29
    • 0035965873 scopus 로고    scopus 로고
    • X-ray and neutron scattering analyses of hydration shells: A molecular interpretation based on sequence predictions and modelling fits
    • S.J. Perkins X-ray and neutron scattering analyses of hydration shells: a molecular interpretation based on sequence predictions and modelling fits Biophys. Chem. 93 2001 129 139
    • (2001) Biophys. Chem. , vol.93 , pp. 129-139
    • Perkins, S.J.1
  • 30
    • 0032488888 scopus 로고    scopus 로고
    • Crystallographic structure of an intact IgG1 monoclonal antibody
    • L.J. Harris, E. Skaletsky, and A. McPherson Crystallographic structure of an intact IgG1 monoclonal antibody J. Mol. Biol. 275 1998 861 872
    • (1998) J. Mol. Biol. , vol.275 , pp. 861-872
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 31
    • 0025812969 scopus 로고
    • Inhibition of Epstein-Barr virus infection in vitro and in vivo by soluble CR2 (CD21) containing two short consensus repeats
    • M.D. Moore, M.J. Cannon, A. Sewall, M. Finlayson, M. Okimoto, and G.R. Nemerow Inhibition of Epstein-Barr virus infection in vitro and in vivo by soluble CR2 (CD21) containing two short consensus repeats J. Virol. 65 1991 3559 3565
    • (1991) J. Virol. , vol.65 , pp. 3559-3565
    • Moore, M.D.1    Cannon, M.J.2    Sewall, A.3    Finlayson, M.4    Okimoto, M.5    Nemerow, G.R.6
  • 32
    • 0032080799 scopus 로고    scopus 로고
    • Blockade of antibody-induced glomerulonephritis with Crry-Ig, a soluble murine complement inhibitor
    • R.J. Quigg, Y. Kozono, D. Berthiaume, A. Lim, D.J. Salant, and A. Weinfeld Blockade of antibody-induced glomerulonephritis with Crry-Ig, a soluble murine complement inhibitor J. Immunol. 160 1998 4553 4560
    • (1998) J. Immunol. , vol.160 , pp. 4553-4560
    • Quigg, R.J.1    Kozono, Y.2    Berthiaume, D.3    Lim, A.4    Salant, D.J.5    Weinfeld, A.6
  • 33
    • 0025739001 scopus 로고
    • A rapid FPLC method for purification of the third component of human and guinea pig complement
    • M. Basta, and C.H. Hammer A rapid FPLC method for purification of the third component of human and guinea pig complement J. Immunol. Methods 142 1991 39 44
    • (1991) J. Immunol. Methods , vol.142 , pp. 39-44
    • Basta, M.1    Hammer, C.H.2
  • 34
    • 0021710078 scopus 로고
    • Analysis of C3-receptor activity on human B-lymphocytes and isolation of the complement receptor type 2 (CR2)
    • K.J. Micklem, R.B. Sim, and E. Sim Analysis of C3-receptor activity on human B-lymphocytes and isolation of the complement receptor type 2 (CR2) Biochem. J. 224 1984 75 86
    • (1984) Biochem. J. , vol.224 , pp. 75-86
    • Micklem, K.J.1    Sim, R.B.2    Sim, E.3
  • 35
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • S.J. Perkins Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences Eur. J. Biochem. 157 1986 169 180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 38
    • 0022787110 scopus 로고
    • Data appraisal, evaluation and display for synchrotron radiation experiments: Hardware and software
    • C. Boulin, R. Kempf, M.H.J. Koch, and S.M. McLaughlin Data appraisal, evaluation and display for synchrotron radiation experiments: hardware and software Nucl. Instrum. Meth. A249 1986 399 407
    • (1986) Nucl. Instrum. Meth. , vol.249 , pp. 399-407
    • Boulin, C.1    Kempf, R.2    Koch, M.H.J.3    McLaughlin, S.M.4
  • 39
    • 44049114919 scopus 로고
    • Upgrading of the SANS instrument D11 at the ILL
    • P. Lindner, R.P. May, and P.A. Timmins Upgrading of the SANS instrument D11 at the ILL Phys. B 180 1992 967 972
    • (1992) Phys. B , vol.180 , pp. 967-972
    • Lindner, P.1    May, R.P.2    Timmins, P.A.3
  • 42
    • 85055706702 scopus 로고
    • Absolute calibration of small angle neutron scattering data
    • G.D. Wignall, and F.S. Bates Absolute calibration of small angle neutron scattering data J. Appl. Crystallog. 20 1987 28 40
    • (1987) J. Appl. Crystallog. , vol.20 , pp. 28-40
    • Wignall, G.D.1    Bates, F.S.2
  • 43
    • 0004283756 scopus 로고
    • Internal publication RAL-89-128, Rutherford Appleton Laboratory, Didcot, UK.
    • Heenan, R. K., King, S. M., Osborn, R. & Stanley, H. B. (1989). COLETTE Users Guide. Internal publication RAL-89-128, Rutherford Appleton Laboratory, Didcot, UK.
    • (1989) COLETTE Users Guide
    • Heenan, R.K.1    King, S.M.2    Osborn, R.3    Stanley, H.B.4
  • 45
    • 0000980676 scopus 로고
    • X-ray small angle scattering with substances of biological interest in diluted solutions
    • O. Kratky X-ray small angle scattering with substances of biological interest in diluted solutions Progr. Biophys. Chem. 13 1963 105 173
    • (1963) Progr. Biophys. Chem. , vol.13 , pp. 105-173
    • Kratky, O.1
  • 46
    • 0026244044 scopus 로고
    • GNOM-a program package for small-angle scattering data-processing
    • A.V. Semenyuk, and D.I. Svergun GNOM-a program package for small-angle scattering data-processing J. Appl. Crystallog. 24 1991 537 540
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 47
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect transform methods using perceptual criteria J. Appl. Crystallog. 25 1992 495 503
    • (1992) J. Appl. Crystallog. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 48
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • J. Philo A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions Anal. Biochem. 279 2000 151 163
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.1
  • 49
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses
    • A.W. Ashton, M.K. Boehm, J.R. Gallimore, M.B. Pepys, and S.J. Perkins Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses J. Mol. Biol. 272 1997 408 422
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 50
    • 0021112502 scopus 로고
    • Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering
    • S.J. Perkins, and H. Weiss Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering J. Mol. Biol. 168 1983 847 866
    • (1983) J. Mol. Biol. , vol.168 , pp. 847-866
    • Perkins, S.J.1    Weiss, H.2
  • 51
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • A.J. Beavil, R.J. Young, B.J. Sutton, and S.J. Perkins Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure Biochemistry 34 1995 14449 14461
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 53
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • J. Garcia de la Torre, M.L. Huertas, and B. Carrasco Calculation of hydrodynamic properties of globular proteins from their atomic-level structure Biophys. J. 78 2000 719 730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garciadela Torre, J.1    Huertas, M.L.2    Carrasco, B.3


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