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Volumn 18, Issue 5, 1999, Pages 1095-1103

Crystal structure of the soluble form of the human Fcγ-receptor IIb: A new member of the immunoglobulin superfamily at 1.7 Å resolution

Author keywords

CD32; Crystal structure; Fc RIIb; IgG receptor

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN;

EID: 0033106166     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (112)

References (49)
  • 1
    • 0017044042 scopus 로고
    • Analysis of mononuclear cell surfaces with fluoresceinated staphylococcal protein A complexed with IgG antibody or heat-aggregated γ-globulin
    • Ades, E.W., Phillips, D.J., Shore, S.L., Gordon, D.S., LaVia, M.F., Black, C.M. and Reimer, C.B. (1976) Analysis of mononuclear cell surfaces with fluoresceinated Staphylococcal protein A complexed with IgG antibody or heat-aggregated γ-globulin. J. Immunol., 117, 2119-2123.
    • (1976) J. Immunol. , vol.117 , pp. 2119-2123
    • Ades, E.W.1    Phillips, D.J.2    Shore, S.L.3    Gordon, D.S.4    LaVia, M.F.5    Black, C.M.6    Reimer, C.B.7
  • 2
    • 0026769620 scopus 로고
    • Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes
    • Amigorena, S. et al. (1992) Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes. Science, 256, 1808-1812.
    • (1992) Science , vol.256 , pp. 1808-1812
    • Amigorena, S.1
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: Tool to format multiple sequence alignments
    • Barton, G.C. (1993) ALSCRIPT: tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.C.1
  • 4
    • 0028265826 scopus 로고
    • Metalloprotease and serine protease are involved in cleavage of CD43, CD44 and CD16 from stimulated human granulocytes
    • Bazil, V. and Strominger, J.L. (1994) Metalloprotease and serine protease are involved in cleavage of CD43, CD44 and CD16 from stimulated human granulocytes. J. Immunol., 152, 1314-1322.
    • (1994) J. Immunol. , vol.152 , pp. 1314-1322
    • Bazil, V.1    Strominger, J.L.2
  • 5
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science, 35, 458-460.
    • (1987) Science , vol.35 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 6
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W.P., Huber, A.H. and Bjorkman, P.J. (1994) Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature, 372, 379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 7
    • 0023678504 scopus 로고
    • Defect in the membrane expression of high affinity 72kD Fcγ receptors on phagocytic cells in four healthy subjects
    • Ceuppens, J.L., Baroja, M.L., van Vaeck, F. and Anderson, C.L. (1988) Defect in the membrane expression of high affinity 72kD Fcγ receptors on phagocytic cells in four healthy subjects. J. Clin. Invest., 82, 571-578.
    • (1988) J. Clin. Invest. , vol.82 , pp. 571-578
    • Ceuppens, J.L.1    Baroja, M.L.2    Van Vaeck, F.3    Anderson, C.L.4
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative computational project, Number 4. (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 9
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution
    • Deisenhofer, J. (1981) Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry, 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 10
    • 0018173811 scopus 로고
    • Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus
    • Deisenhofer, J., Jones, T.A., Huber, R., Sjodahl, J. and Sjoquist, J. (1978) Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus. Z. Physiol. Chem., 359, 975-985.
    • (1978) Z. Physiol. Chem. , vol.359 , pp. 975-985
    • Deisenhofer, J.1    Jones, T.A.2    Huber, R.3    Sjodahl, J.4    Sjoquist, J.5
  • 11
    • 0025286913 scopus 로고
    • Distribution, inducibility and biological function of the cloned and expressed human βFc receptor II
    • Engelhardt, W., Geerds, C. and Frey, J. (1990) Distribution, inducibility and biological function of the cloned and expressed human βFc receptor II. Eur. J. Immunol., 20, 1367-1377.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 1367-1377
    • Engelhardt, W.1    Geerds, C.2    Frey, J.3
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr., A47, 392-400.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • Gabb, H.A., Jackson, R.M. and Sternberg, M.J.E. (1997) Modelling protein docking using shape complementarity, electrostatics and biochemical information. J. Mol. Biol., 272, 106-120.
    • (1997) J. Mol. Biol. , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.E.3
  • 18
    • 0027456571 scopus 로고
    • Structural motifs involved in human IgG antibody effector functions
    • Greenwood, J., Clark, M. and Waldmann, H. (1993) Structural motifs involved in human IgG antibody effector functions. Eur. J. Immunol., 23, 1098-1104.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1098-1104
    • Greenwood, J.1    Clark, M.2    Waldmann, H.3
  • 21
    • 0024390828 scopus 로고
    • The Fc and not CD4 receptor mediates antibody enhancement of HIV infection in human cells
    • Homsy, J., Meyer, M., Tateno, M., Clarkson, S. and Levy, J.A. (1989) The Fc and not CD4 receptor mediates antibody enhancement of HIV infection in human cells. Science, 244, 1357-1360.
    • (1989) Science , vol.244 , pp. 1357-1360
    • Homsy, J.1    Meyer, M.2    Tateno, M.3    Clarkson, S.4    Levy, J.A.5
  • 23
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • Huber, R., Deisenhofer, J., Colman, P.M., Matsushima, M. and Palm, W. (1976) Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature, 264, 415-420.
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4    Palm, W.5
  • 24
    • 0028339125 scopus 로고
    • Identification of the IgG binding site of the human low affinity receptor for IgG FcγRII
    • Hulett, M.D. Witort, E., Brinkworth, R.I., McKenzie, I.F.C. and Hogarth, P.M. (1994) Identification of the IgG binding site of the human low affinity receptor for IgG FcγRII. J. Biol. Chem., 269, 15287-15293.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15287-15293
    • Hulett, M.D.1    Witort, E.2    Brinkworth, R.I.3    McKenzie, I.F.C.4    Hogarth, P.M.5
  • 26
    • 0025666553 scopus 로고
    • Molecular definition of interaction sites on human IgG for Fc receptors (huFc γR)
    • Jefferis, R., Lund, J. and Pound, J. (1990) Molecular definition of interaction sites on human IgG for Fc receptors (huFc γR). Mol. Immunol., 27, 1237-1240.
    • (1990) Mol. Immunol. , vol.27 , pp. 1237-1240
    • Jefferis, R.1    Lund, J.2    Pound, J.3
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0028173093 scopus 로고
    • Similarities between protein 3-D structures
    • Lessel, U. and Schomburg, D. (1994) Similarities between protein 3-D structures. Protein Eng., 7, 1175-1187.
    • (1994) Protein Eng. , vol.7 , pp. 1175-1187
    • Lessel, U.1    Schomburg, D.2
  • 31
    • 0025361063 scopus 로고
    • Human IgG Fc receptor II mediates antibody-dependent enhancement of dengue virus infection
    • Littaua, R., Kurane, I. and Ennis, F.A. (1990) Human IgG Fc receptor II mediates antibody-dependent enhancement of dengue virus infection. J. Immunol., 144, 3183-3186.
    • (1990) J. Immunol. , vol.144 , pp. 3183-3186
    • Littaua, R.1    Kurane, I.2    Ennis, F.A.3
  • 32
    • 0028946387 scopus 로고
    • Potential role of FcγR in early development of murine lymphoid cells: Evidence for functional interaction between FcγR on pre-thymocytes and an alternative, non-Ig ligand on thymic stromal cells
    • Lynch, R.G., Hagen, M., Mueller, A. and Sandor, M. (1995) Potential role of FcγR in early development of murine lymphoid cells: Evidence for functional interaction between FcγR on pre-thymocytes and an alternative, non-Ig ligand on thymic stromal cells. Immunol. Lett., 44, 105-109.
    • (1995) Immunol. Lett. , vol.44 , pp. 105-109
    • Lynch, R.G.1    Hagen, M.2    Mueller, A.3    Sandor, M.4
  • 33
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A. and Murphy, M.E.P. (1994) Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr., D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 34
    • 0026675654 scopus 로고
    • Transmembrane signaling: The joy of aggregation
    • Metzger, H. (1992a) Transmembrane signaling: The joy of aggregation. J. Immunol., 149, 1477-1487.
    • (1992) J. Immunol. , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 35
    • 0026611231 scopus 로고
    • The receptor with high affinity for IgE
    • Metzger, H. (1992b) The receptor with high affinity for IgE. Immunol. Rev., 125, 37-48.
    • (1992) Immunol. Rev. , vol.125 , pp. 37-48
    • Metzger, H.1
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 37
    • 0028988449 scopus 로고
    • Interaction of Fcγ receptor IIIB with complement receptor type 3 in fibroblast transfectants: Evidence from lateral diffusion and resonance energy transfer studies
    • Poo, H., Kraus, J.C., Mayo-Bond, L., Todd, R.F. and Petty, H.R. (1995) Interaction of Fcγ receptor IIIB with complement receptor type 3 in fibroblast transfectants: evidence from lateral diffusion and resonance energy transfer studies. J. Mol. Biol., 247, 597-603.
    • (1995) J. Mol. Biol. , vol.247 , pp. 597-603
    • Poo, H.1    Kraus, J.C.2    Mayo-Bond, L.3    Todd, R.F.4    Petty, H.R.5
  • 41
    • 0026507779 scopus 로고
    • Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of human Fc γ receptor
    • Sarmay, G., Lund, J., Rozsnyay, Z., Gergely, J. and Jefferis, R. (1992) Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of human Fc γ receptor. Mol. Immunol., 29, 633-639.
    • (1992) Mol. Immunol. , vol.29 , pp. 633-639
    • Sarmay, G.1    Lund, J.2    Rozsnyay, Z.3    Gergely, J.4    Jefferis, R.5
  • 42
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlen, M. and Jones, T.A. (1995) Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure, 3, 265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlen, M.3    Jones, T.A.4
  • 43
    • 0020578878 scopus 로고
    • Polymorphism in mitogenic effect of IgG1 monoclonal antibodies against T3 antigen on human T cells
    • Tax, W.J.M., Willems, H.W., Reekers, P.P.M., Capel, P.J.A. and Koene, R.A.P. (1983) Polymorphism in mitogenic effect of IgG1 monoclonal antibodies against T3 antigen on human T cells. Nature, 304, 445-447.
    • (1983) Nature , vol.304 , pp. 445-447
    • Tax, W.J.M.1    Willems, H.W.2    Reekers, P.P.M.3    Capel, P.J.A.4    Koene, R.A.P.5
  • 44
    • 0344093769 scopus 로고
    • PhD thesis. TU München, Germany
    • Turk, D. (1992) PhD thesis. TU München, Germany.
    • (1992)
    • Turk, D.1
  • 45
    • 0027204803 scopus 로고
    • Human IgG Fc receptor heterogeneity: Molecular aspects and clinical implications
    • van de Winkel, J.G.J. and Capel, P.J.A. (1993) Human IgG Fc receptor heterogeneity: Molecular aspects and clinical implications. Immunol. Today, 14, 215-221.
    • (1993) Immunol. Today , vol.14 , pp. 215-221
    • Van De Winkel, J.G.J.1    Capel, P.J.A.2
  • 46
    • 0024796884 scopus 로고
    • Recombinant soluble receptors for the Fcγ portion inhibit antibody production in vitro
    • Varin, N., Sautès, C., Galinha, A., Even, J., Hogarth, P.M. and Fridman, W.H. (1989) Recombinant soluble receptors for the Fcγ portion inhibit antibody production in vitro. Eur. J. Immunol., 19, 2263-2268.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2263-2268
    • Varin, N.1    Sautès, C.2    Galinha, A.3    Even, J.4    Hogarth, P.M.5    Fridman, W.H.6
  • 47
    • 0025198478 scopus 로고
    • Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
    • Wang, J.H. et al. (1990) Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature, 348, 411-418.
    • (1990) Nature , vol.348 , pp. 411-418
    • Wang, J.H.1
  • 48
    • 0032512668 scopus 로고    scopus 로고
    • Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins
    • Yang, Z., Delgado, R., Xu, L., Todd, R.F., Nabel, E.G., Sanchez, A. and Nabel, G.J. (1998) Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins. Science, 279, 983-984.
    • (1998) Science , vol.279 , pp. 983-984
    • Yang, Z.1    Delgado, R.2    Xu, L.3    Todd, R.F.4    Nabel, E.G.5    Sanchez, A.6    Nabel, G.J.7
  • 49
    • 0027231055 scopus 로고
    • Cocapping of the leukoadhesin molecules complement receptor type 3 and lymphocyte function-associated antigen-1 with Fcγ receptor III on human neutrophils. Possible role of lectin-like interactions
    • Zhou, M.-J., Todd, R.F., van de Winkel, J.G.J. and Petty, H.R. (1993) Cocapping of the leukoadhesin molecules complement receptor type 3 and lymphocyte function-associated antigen-1 with Fcγ receptor III on human neutrophils. Possible role of lectin-like interactions. J. Immunol., 150, 3030-3041.
    • (1993) J. Immunol. , vol.150 , pp. 3030-3041
    • Zhou, M.-J.1    Todd, R.F.2    Van De Winkel, J.G.J.3    Petty, H.R.4


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