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Volumn 4, Issue 2, 2004, Pages 89-99

Human antibody-Fc receptor interactions illuminated by crystal structures

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; FC ALPHA RECEPTOR I; FC EPSILON RECEPTOR I; FC EPSILON RECEPTOR II; FC EPSILON RECEPTOR IIA; FC EPSILON RECEPTOR IIB; FC RECEPTOR; FC RECEPTOR I; FC RECEPTOR IA; FC RECEPTOR II; FC RECEPTOR IIA; FC RECEPTOR IIB; FC RECEPTOR IIC; FC RECEPTOR III; FC RECEPTOR IIIA; FC RECEPTOR IIIB; IMMUNOGLOBULIN A; IMMUNOGLOBULIN A1; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN M; UNCLASSIFIED DRUG;

EID: 1142298744     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1266     Document Type: Review
Times cited : (298)

References (97)
  • 1
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M. & Palm, W. Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 264, 415-420 (1976).
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4    Palm, W.5
  • 2
    • 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. 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).
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 4
    • 0033673325 scopus 로고    scopus 로고
    • Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains
    • Wurzburg, B. A., Garman, S. C. & Jardetzky, T. S. Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains. Immunity 13, 375-385 (2000).
    • (2000) Immunity , vol.13 , pp. 375-385
    • Wurzburg, B.A.1    Garman, S.C.2    Jardetzky, T.S.3
  • 5
    • 0036308980 scopus 로고    scopus 로고
    • The crystal structure of IgE reveals an asymmetrically bent conformation
    • 2 was determined and compared with that of the Fc region lacking the Cε2 domains, both uncomplexed and complexed to FcεRI.
    • (2002) Nature Immunol. , vol.3 , pp. 681-686
    • Wan, T.1
  • 6
    • 0037497304 scopus 로고    scopus 로고
    • Insights into IgA-mediated immune responses from the crystal structures of human FcαRI and its complex with IgA1-Fc
    • Herr, A. B., Ballister, E. R. & Bjorkman, P. J. Insights into IgA-mediated immune responses from the crystal structures of human FcαRI and its complex with IgA1-Fc. Nature 423, 614-620 (2003). This paper reported the X-ray crystal structure of IgA complexed with FcαRI.
    • (2003) Nature , vol.423 , pp. 614-620
    • Herr, A.B.1    Ballister, E.R.2    Bjorkman, P.J.3
  • 8
    • 0025939199 scopus 로고
    • Conformations of IgE bound to its receptor FcεRI and in solution
    • Zheng, Y., Shopes, B., Holowka, D. & Baird, B. Conformations of IgE bound to its receptor FcεRI and in solution. Biochemistry 30, 9125-9132 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9125-9132
    • Zheng, Y.1    Shopes, B.2    Holowka, D.3    Baird, B.4
  • 9
    • 0026679890 scopus 로고
    • The three-dimensional structure of an intact monoclonal antibody for canine lymphoma
    • Harris, L. J. et al. The three-dimensional structure of an intact monoclonal antibody for canine lymphoma. Nature 360, 369-372 (1992).
    • (1992) Nature , vol.360 , pp. 369-372
    • Harris, L.J.1
  • 10
    • 0032488888 scopus 로고    scopus 로고
    • Crystallographic structure of an intact IgG1 monoclonal antibody
    • Harris, L. J., Skaletsky, E. & McPherson, A. Crystallographic structure of an intact IgG1 monoclonal antibody. J. Mol. Biol. 275, 861-872 (1998).
    • (1998) J. Mol. Biol. , vol.275 , pp. 861-872
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 11
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IgG against HIV-1: A template for vaccine design
    • Saphire, E. O. et al. Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 293, 1155-1159 (2001).
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1
  • 12
    • 0036304632 scopus 로고    scopus 로고
    • Contrasting IgG structures reveal extreme asymmetry and flexibility
    • Saphire, E. O. et al. Contrasting IgG structures reveal extreme asymmetry and flexibility. J. Mol. Biol. 319, 9-18 (2002). This paper provides insights into the structure and flexibility of IgG through comparison of the X-ray crystal structures of intact IgG molecules.
    • (2002) J. Mol. Biol. , vol.319 , pp. 9-18
    • Saphire, E.O.1
  • 13
    • 0015057896 scopus 로고
    • Further studies on the ultrastructure of dimeric IgA of human origin
    • Bloth, B. & Svehag, S. E. Further studies on the ultrastructure of dimeric IgA of human origin. J. Exp. Med. 133, 1035-1042 (1971).
    • (1971) J. Exp. Med. , vol.133 , pp. 1035-1042
    • Bloth, B.1    Svehag, S.E.2
  • 14
    • 0015239712 scopus 로고
    • Electron microscope examination of free molecules and of their complexes with antigen
    • Munn, E. A., Feinstein A. & Munro A. J. Electron microscope examination of free molecules and of their complexes with antigen. Nature 231, 527-529 (1971).
    • (1971) Nature , vol.231 , pp. 527-529
    • Munn, E.A.1    Feinstein, A.2    Munro, A.J.3
  • 15
    • 0015242948 scopus 로고
    • Electron microscopy of human and mouse myeloma serum IgA
    • Dourmashkin, R. R., Virella, G. & Parkhouse, R. M. Electron microscopy of human and mouse myeloma serum IgA. J. Mol. Biol. 56, 207-208 (1971).
    • (1971) J. Mol. Biol. , vol.56 , pp. 207-208
    • Dourmashkin, R.R.1    Virella, G.2    Parkhouse, R.M.3
  • 16
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
    • Roux, K. H., Strelets, L., Brekke, O. H., Sandlie, I. & Michaelsen, T. E. Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: a role for flexibility and geometry. J. Immunol. 181, 4083-4090 (1998).
    • (1998) J. Immunol. , vol.181 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 17
    • 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
    • Boehm, M. K., Woof, J. M., Kerr, M. A. & Perkins, S. J. 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, 1421-1447 (1999).
    • (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
  • 18
    • 0026787987 scopus 로고
    • Dynamic conformations compared for IgE and IgG1 in solution and bound to receptors
    • Zheng, Y., Shopes, B., Holowka, D. & Baird, B. Dynamic conformations compared for IgE and IgG1 in solution and bound to receptors. Biochemistry 31, 7446-7456 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7446-7456
    • Zheng, Y.1    Shopes, B.2    Holowka, D.3    Baird, B.4
  • 19
    • 0026657624 scopus 로고
    • Human antibody effector function
    • Burton, D. R. & Woof, J. M. Human antibody effector function. Adv. Immunol. 51, 1-84 (1992).
    • (1992) Adv. Immunol. , vol.51 , pp. 1-84
    • Burton, D.R.1    Woof, J.M.2
  • 21
    • 0035046581 scopus 로고    scopus 로고
    • Human receptors for immunoglobulin G
    • Salmon, J. E. & Pricop, L. Human receptors for immunoglobulin G. Arthritis Rheum. 44, 739-750 (2001).
    • (2001) Arthritis Rheum. , vol.44 , pp. 739-750
    • Salmon, J.E.1    Pricop, L.2
  • 23
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth, M. Antigen receptor tail clue. Nature 338, 383-384 (1989).
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 25
    • 0026504388 scopus 로고
    • The gene for the human IgA Fc receptor maps to 19q13. 4
    • Kremer, E. J. et al. The gene for the human IgA Fc receptor maps to 19q13. 4. Hum. Genet. 89, 107-108 (1992).
    • (1992) Hum. Genet. , vol.89 , pp. 107-108
    • Kremer, E.J.1
  • 26
    • 0032806019 scopus 로고    scopus 로고
    • Organization of the leukocyte receptor cluster (LRC) on human chromosome 19q13. 4
    • Wende, H., Colonna, M., Ziegler, A. & Volz, A. Organization of the leukocyte receptor cluster (LRC) on human chromosome 19q13. 4. Mamm. Genome 10, 154-160 (1999).
    • (1999) Mamm. Genome , vol.10 , pp. 154-160
    • Wende, H.1    Colonna, M.2    Ziegler, A.3    Volz, A.4
  • 27
    • 0036630357 scopus 로고    scopus 로고
    • Molecular versatility of antibodies
    • Metzger, H. Molecular versatility of antibodies. Immunol. Rev. 185, 186-205 (2002).
    • (2002) Immunol. Rev. , vol.185 , pp. 186-205
    • Metzger, H.1
  • 28
    • 0000457253 scopus 로고
    • Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation
    • Segal, D. M., Taurog, J. D. & Metzger, H. Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation. Proc. Natl Acad Sci. USA 74, 2993-2997 (1977).
    • (1977) Proc. Natl. Acad Sci. USA , vol.74 , pp. 2993-2997
    • Segal, D.M.1    Taurog, J.D.2    Metzger, H.3
  • 29
    • 0036888683 scopus 로고    scopus 로고
    • Molecular adapters in FcεRI signaling and the allergic response
    • Rivera, J. Molecular adapters in FcεRI signaling and the allergic response. Curr. Opin. Immunol. 14, 688-693 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 688-693
    • Rivera, J.1
  • 30
    • 0026601947 scopus 로고
    • Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases
    • Eiseman, E. & Bolen, J. B. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355, 78-80 (1992).
    • (1992) Nature , vol.355 , pp. 78-80
    • Eiseman, E.1    Bolen, J.B.2
  • 31
    • 0031973743 scopus 로고    scopus 로고
    • Physical and functional association of FcαR with protein tyrosine kinase Lyn
    • Guile, H., Samstag, A., Eibl, M. M. & Wolf, H. M. Physical and functional association of FcαR with protein tyrosine kinase Lyn. Blood 91, 383-391 (1998).
    • (1998) Blood , vol.91 , pp. 383-391
    • Guile, H.1    Samstag, A.2    Eibl, M.M.3    Wolf, H.M.4
  • 32
    • 0036180132 scopus 로고    scopus 로고
    • Interactions of integrins with their partner proteins in leukocyte membranes
    • Petty, H. R., Worth, R. G. & Todd, R. F. Interactions of integrins with their partner proteins in leukocyte membranes. Immunol. Res. 25, 75-95 (2002).
    • (2002) Immunol. Res. , vol.25 , pp. 75-95
    • Petty, H.R.1    Worth, R.G.2    Todd, R.F.3
  • 33
    • 0033564274 scopus 로고    scopus 로고
    • Human immunoglobulin A receptor (FcαRI, CD89) function in transgenic mice requires both FcR γ chain and CR3 (CD11b/CD18)
    • van Egmond, M. et al. Human immunoglobulin A receptor (FcαRI, CD89) function in transgenic mice requires both FcR γ chain and CR3 (CD11b/CD18). Blood 93, 4387-4394 (1999).
    • (1999) Blood , vol.93 , pp. 4387-4394
    • Van Egmond, M.1
  • 34
    • 0036786472 scopus 로고    scopus 로고
    • Mac-1 (CD11b/CD18) as accessory molecule for FcαR (CD89) binding of IgA
    • van Spriel, A. B., Leusen, J. H., Vile, H. & van de Winkel, J. G. J. Mac-1 (CD11b/CD18) as accessory molecule for FcαR (CD89) binding of IgA. J. Immunol. 189, 3831-3836 (2002).
    • (2002) J. Immunol. , vol.189 , pp. 3831-3836
    • Van Spriel, A.B.1    Leusen, J.H.2    Vile, H.3    Van De Winkel, J.G.J.4
  • 35
    • 0032937238 scopus 로고    scopus 로고
    • Crystal structure of the human leukocyte Fc receptor, FcγRIIa
    • Maxwell, K. F. et al. Crystal structure of the human leukocyte Fc receptor, FcγRIIa. Nature Struct. Biol. 6, 437-442 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 437-442
    • Maxwell, K.F.1
  • 36
    • 0035827222 scopus 로고    scopus 로고
    • Molecular basis for immune complex recognition: A comparison of Fc-receptor structures
    • Sondermann, P., Kaiser, J. & Jacob, U. Molecular basis for immune complex recognition: a comparison of Fc-receptor structures. J. Mol. Biol. 309, 737-749 (2001).
    • (2001) J. Mol. Biol. , vol.309 , pp. 737-749
    • Sondermann, P.1    Kaiser, J.2    Jacob, U.3
  • 37
    • 0033106166 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of the human Fcγ-receptor IIb: A new member of the immunoglobulin superfamily at 1.7 Å resolution
    • Sondermann, P., Huber, R. & Jacob, U. Crystal structure of the soluble form of the human Fcγ-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 Å resolution. EMBO J. 18, 1095-1103 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1095-1103
    • Sondermann, P.1    Huber, R.2    Jacob, U.3
  • 38
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex
    • Sondermann, P., Huber, R., Oosthuizen, V. & Jacob, U. The 3. 2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex. Nature 406, 267-273 (2000). This paper and reference 40 describe the X-ray crystal structure of the complex between IgG1 and FCγRIII.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 39
    • 0033673344 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of a human FcγRIII
    • Zheng, Y. et al. Crystal structure of the extracellular domain of a human FcγRIII. Immunity 13, 387-395 (2000).
    • (2000) Immunity , vol.13 , pp. 387-395
    • Zheng, Y.1
  • 41
    • 0032419721 scopus 로고    scopus 로고
    • Crystal structure of the human high-affinity IgE receptor
    • Garman, S. C., Kinet, J.-P. & Jardetzky, T. S. Crystal structure of the human high-affinity IgE receptor. Cell 95, 951-961 (1998).
    • (1998) Cell , vol.95 , pp. 951-961
    • Garman, S.C.1    Kinet, J.-P.2    Jardetzky, T.S.3
  • 42
    • 0035979716 scopus 로고    scopus 로고
    • The analysis of the human high affinity IgE receptor FcεRIα from multiple crystal forms
    • Garman, S. C., Sechi, S., Kinet, J. P. & Jardetzky, T. S. The analysis of the human high affinity IgE receptor FcεRIα from multiple crystal forms. J. Mol. Biol. 311, 1049-1062 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 1049-1062
    • Garman, S.C.1    Sechi, S.2    Kinet, J.P.3    Jardetzky, T.S.4
  • 43
    • 0041344597 scopus 로고    scopus 로고
    • Crystal structure of the ectodomain of human FcαRI
    • Ding, Y. et al. Crystal structure of the ectodomain of human FcαRI. J. Biol. Chem. 278, 27966-27970 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 27966-27970
    • Ding, Y.1
  • 44
    • 0030931534 scopus 로고    scopus 로고
    • Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors
    • Fan, Q. R. et al. Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature 389, 96-100 (1997).
    • (1997) Nature , vol.389 , pp. 96-100
    • Fan, Q.R.1
  • 45
    • 0033636273 scopus 로고    scopus 로고
    • Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2)
    • Chapman, T. L., Heikema, A. P., West, A. P. & Bjorkman, P. J. Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2). Immunity 13, 727-736 (2000).
    • (2000) Immunity , vol.13 , pp. 727-736
    • Chapman, T.L.1    Heikema, A.P.2    West, A.P.3    Bjorkman, P.J.4
  • 46
    • 0031674586 scopus 로고    scopus 로고
    • The second and third extracellular domains of FcγRI (CD64) confer the unique high affinity binding of IgG2a
    • Hulett, M. D. & Hogarth, P. M. The second and third extracellular domains of FcγRI (CD64) confer the unique high affinity binding of IgG2a. Mol. Immunol. 35, 989-996 (1998).
    • (1998) Mol. Immunol. , vol.35 , pp. 989-996
    • Hulett, M.D.1    Hogarth, P.M.2
  • 47
    • 0028339125 scopus 로고
    • Identification of the IgG binding site of the human low affinity receptor for IgG FcγRII. Enhancement and ablation of binding by site-directed mutagenesis
    • Hulett, M. D., Witort, E., Brinkworth, R. I., McKenzie, I. F. & Hogarth, P. M. Identification of the IgG binding site of the human low affinity receptor for IgG FcγRII. Enhancement and ablation of binding by site-directed mutagenesis. J. Biol. Chem. 269, 15287-15293 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 15287-15293
    • Hulett, M.D.1    Witort, E.2    Brinkworth, R.I.3    McKenzie, I.F.4    Hogarth, P.M.5
  • 48
    • 0029099943 scopus 로고
    • Multiple regions of human FcγRII (CD32) contribute to the binding of IgG
    • Hulett, M. D., Witort, E., Brinkworth, R. I., McKenzie, I. F. & Hogarth, P. M. Multiple regions of human FcγRII (CD32) contribute to the binding of IgG. J. Biol. Chem. 270, 21188-21194 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21188-21194
    • Hulett, M.D.1    Witort, E.2    Brinkworth, R.I.3    McKenzie, I.F.4    Hogarth, P.M.5
  • 49
    • 0030045239 scopus 로고    scopus 로고
    • The IgG binding site of human FcγRII receptor involves CC' and FG loops of the membrane-proximal domain
    • Tamm, A., Kister, A., Nolte, K. U., Gessner, J. E. & Schmidt, R. E. The IgG binding site of human FcγRII receptor involves CC' and FG loops of the membrane-proximal domain. J. Biol. Chem. 271, 3659-3666 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3659-3666
    • Tamm, A.1    Kister, A.2    Nolte, K.U.3    Gessner, J.E.4    Schmidt, R.E.5
  • 50
    • 0022611355 scopus 로고
    • Localisation of the monocyte-binding region on human immunoglobulin G
    • Woof, J. M., Partridge, L. J., Jefferis R. & Burton, D. R. Localisation of the monocyte-binding region on human immunoglobulin G. Mol. Immunol. 23, 319-330 (1986).
    • (1986) Mol. Immunol. , vol.23 , pp. 319-330
    • Woof, J.M.1    Partridge, L.J.2    Jefferis, R.3    Burton, D.R.4
  • 51
    • 0023933120 scopus 로고
    • Localization of the binding site for the human high-affinity Fc receptor on IgG
    • Duncan, A. R., Woof, J. M., Partridge, L. J., Burton, D. R. & Winter, G. Localization of the binding site for the human high-affinity Fc receptor on IgG. Nature 332, 563-564 (1988).
    • (1988) Nature , vol.332 , pp. 563-564
    • Duncan, A.R.1    Woof, J.M.2    Partridge, L.J.3    Burton, D.R.4    Winter, G.5
  • 52
    • 0026050344 scopus 로고
    • Human FcγRI and FcγRII interact with distinct but overlapping sites on human IgG
    • Lund, J. et al. Human FcγRI and FcγRII interact with distinct but overlapping sites on human IgG. J. Immunol. 147, 2657-2662 (1991).
    • (1991) J. Immunol. , vol.147 , pp. 2657-2662
    • Lund, J.1
  • 53
    • 0025943212 scopus 로고
    • Identification of the Fcγ-receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies
    • Chappel, M. S. et al. Identification of the Fcγ-receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies. Proc. Natl Acad. Sci. USA 88, 9036-9040 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9036-9040
    • Chappel, M.S.1
  • 54
    • 0025762394 scopus 로고
    • The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
    • Canfield, S. M. & Morrison, S. L. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J. Exp. Med. 173, 1483-1491 (1991).
    • (1991) J. Exp. Med. , vol.173 , pp. 1483-1491
    • Canfield, S.M.1    Morrison, S.L.2
  • 56
    • 0031443213 scopus 로고    scopus 로고
    • Participation of the N-terminal region of Cε3 in the binding of human IgE to its high-affinity receptor FcεeRI
    • Henry, A. J. et al. Participation of the N-terminal region of Cε3 in the binding of human IgE to its high-affinity receptor FcεeRI, Biochemistry 38, 15568-15578 (1997).
    • (1997) Biochemistry , vol.38 , pp. 15568-15578
    • Henry, A.J.1
  • 57
    • 0032922876 scopus 로고    scopus 로고
    • The structural basis of human IgE-Fc receptor interactions
    • Sayers I. & Helm, B. A. The structural basis of human IgE-Fc receptor interactions. Clin. Exp. Allergy 29, 585-594 (1999).
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 585-594
    • Sayers, I.1    Helm, B.A.2
  • 58
    • 0034744342 scopus 로고    scopus 로고
    • The structure of the IgE Cε2 domain and its role in stabilizing the complex with its high-affinity receptor FcεRIα
    • McDonnell, J. M. et al. The structure of the IgE Cε2 domain and its role in stabilizing the complex with its high-affinity receptor FcεRIα. Nature Struct. Biol. 8, 437-441 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 437-441
    • McDonnell, J.M.1
  • 59
    • 0029740925 scopus 로고    scopus 로고
    • A conformational rearrangement upon binding of IgE to its high affinity receptor
    • Sechi, S., Roller, P. P., Willett-Brown, J. & Kinet, J.-P. A conformational rearrangement upon binding of IgE to its high affinity receptor. J. Biol. Chem. 32, 19256-19263 (1996).
    • (1996) J. Biol. Chem. , vol.32 , pp. 19256-19263
    • Sechi, S.1    Roller, P.P.2    Willett-Brown, J.3    Kinet, J.-P.4
  • 60
    • 0033428763 scopus 로고    scopus 로고
    • Interaction of human IgE with FcεRIa exposes hidden epitopes on IgE
    • Nechansky, A. et al. Interaction of human IgE with FcεRIa exposes hidden epitopes on IgE. Int. Arch. Allergy Immunol. 120, 295-302 (1999).
    • (1999) Int. Arch. Allergy Immunol. , vol.120 , pp. 295-302
    • Nechansky, A.1
  • 61
    • 0029924133 scopus 로고    scopus 로고
    • Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Cα2 and Cα3 in human IgA1
    • Carayannopoulos, L., Hexham, J. M. & Capra, J. D. Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Cα2 and Cα3 in human IgA1. J. Exp. Med. 183, 1579-1586 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 1579-1586
    • Carayannopoulos, L.1    Hexham, J.M.2    Capra, J.D.3
  • 62
    • 0033551694 scopus 로고    scopus 로고
    • Identification of residues in the CH2/CH3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαR) CD89
    • Pleass, R. J., Dunlop, J. I., Anderson, C. M. & Woof, J. M. Identification of residues in the CH2/CH3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαR) CD89. J. Biol. Chem. 274, 23508-23514 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23508-23514
    • Pleass, R.J.1    Dunlop, J.I.2    Anderson, C.M.3    Woof, J.M.4
  • 63
    • 0033557751 scopus 로고    scopus 로고
    • Identification of residues in the first domain of human Fcα receptor essential for interaction with IgA
    • Wines, B. D. et al. Identification of residues in the first domain of human Fcα receptor essential for interaction with IgA. J. Immunol. 162, 2146-2153 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 2146-2153
    • Wines, B.D.1
  • 64
    • 0033532545 scopus 로고    scopus 로고
    • Immunoglobulin-binding sites of human FcαRI (CD89) and bovine Fcγ2R are located in their membrane-distal extracellular domains
    • Morton, H. C. et al. Immunoglobulin-binding sites of human FcαRI (CD89) and bovine Fcγ2R are located in their membrane-distal extracellular domains. J. Exp. Med. 189, 1715-1722 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1715-1722
    • Morton, H.C.1
  • 65
    • 0035253436 scopus 로고    scopus 로고
    • The interaction of FcαRI with IgA and its implications for ligand binding by immunoreceptors of the leukocyte receptor cluster
    • Wines, B. D., Sardjono, C. T., Trist, H. M., Lay, C.-S. & Hogarth, P. M. The interaction of FcαRI with IgA and its implications for ligand binding by immunoreceptors of the leukocyte receptor cluster. J. Immunol. 166, 1781-1789 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 1781-1789
    • Wines, B.D.1    Sardjono, C.T.2    Trist, H.M.3    Lay, C.-S.4    Hogarth, P.M.5
  • 66
    • 0037470618 scopus 로고    scopus 로고
    • Bivalent binding of IgA1 to FcαRI suggests a mechanism for cytokine activation of IgA phagocytosis
    • Herr, A. B., White, C. L., Milbum, C., Wu, C. & Bjorkman, P. J. Bivalent binding of IgA1 to FcαRI suggests a mechanism for cytokine activation of IgA phagocytosis. J. Mol. Biol. 327, 645-657 (2003). Using analytical ultracentrifugation and equilibrium gel-filtration experiments, this study indicated that, in solution, two molecules of IgA1 can bind to one molecule of FcαRI.
    • (2003) J. Mol. Biol. , vol.327 , pp. 645-657
    • Herr, A.B.1    White, C.L.2    Milbum, C.3    Wu, C.4    Bjorkman, P.J.5
  • 67
    • 0038803982 scopus 로고    scopus 로고
    • Limited role of charge matching in the interaction of human immunoglobulin A (IgA) with the IgA Fc receptor (FcαRI) CD89
    • Pleass, R. J., Dehal, P. K., Lewis, M. J. & Woof, J. M. Limited role of charge matching in the interaction of human immunoglobulin A (IgA) with the IgA Fc receptor (FcαRI) CD89. Immunology 109, 331-335 (2003).
    • (2003) Immunology , vol.109 , pp. 331-335
    • Pleass, R.J.1    Dehal, P.K.2    Lewis, M.J.3    Woof, J.M.4
  • 68
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation on FcαR interactions
    • Mattu, T. S. et al. The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation on FcαR interactions. J. Biol. Chem. 273, 2260-2272 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.S.1
  • 69
    • 0033625773 scopus 로고    scopus 로고
    • FcαRI-positive liver Kupffer cells: Reappraisal of the function of immunoglobulin A in immunity
    • van Egmond, M. et al. FcαRI-positive liver Kupffer cells: reappraisal of the function of immunoglobulin A in immunity. Nature Med. 8, 680-685 (2000).
    • (2000) Nature Med. , vol.8 , pp. 680-685
    • Van Egmond, M.1
  • 70
    • 0025202096 scopus 로고
    • The specificity of the human neutrophil IgA receptor (FcαR) determined by measurement of chemiluminescence induced by serum or secretory IgA1 or IgA2
    • Stewart, W. W. & Kerr, M. A. The specificity of the human neutrophil IgA receptor (FcαR) determined by measurement of chemiluminescence induced by serum or secretory IgA1 or IgA2. Immunology 71, 328-334 (1990).
    • (1990) Immunology , vol.71 , pp. 328-334
    • Stewart, W.W.1    Kerr, M.A.2
  • 71
    • 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. & Jones, T. A. Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3, 265-278 (1995).
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlen, M.3    Jones, T.A.4
  • 72
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8 Å of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding
    • Martin, W. L., West, A. P. Jr, Gen, L. & Bjorkman, P. J. Crystal structure at 2.8 Å of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding. Mol. Cell 7, 867-877 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 867-877
    • Martin, W.L.1    West Jr., A.P.2    Gen, L.3    Bjorkman, P.J.4
  • 73
    • 0030938368 scopus 로고    scopus 로고
    • Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction
    • Corper, A. L. et al. Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction. Nature Struct. Biol. 4, 374-381 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 374-381
    • Corper, A.L.1
  • 74
    • 0035896552 scopus 로고    scopus 로고
    • Streptococcal IgA-binding proteins bind in the Cα2-Cα3 interdomain region and inhibit binding of IgA to human CD89
    • Pleass, R. J., Areschoug, T., Lindahl, G. & Woof, J. M. Streptococcal IgA-binding proteins bind in the Cα2-Cα3 interdomain region and inhibit binding of IgA to human CD89. J. Biol. Chem. 276, 8197-8204 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 8197-8204
    • Pleass, R.J.1    Areschoug, T.2    Lindahl, G.3    Woof, J.M.4
  • 75
    • 0021857415 scopus 로고
    • Immunoglobulin G functional sites
    • Burton, D. R. Immunoglobulin G: functional sites. Mol. Immunol. 22, 161-206 (1985).
    • (1985) Mol. Immunol. , vol.22 , pp. 161-206
    • Burton, D.R.1
  • 76
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W. L., Ultsch, M. H., de Vos, A. M. & Wells, J. A. Convergent solutions to binding at a protein-protein interface. Science 287, 1279-1283 (2000).
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 77
    • 0036010538 scopus 로고    scopus 로고
    • Recognition of immunoglobulins by Fcγ receptors
    • Radaev, S. & Sun, P. Recognition of immunoglobulins by Fcγ receptors. Mol. Immunol. 38, 1073-1083 (2001).
    • (2001) Mol. Immunol. , vol.38 , pp. 1073-1083
    • Radaev, S.1    Sun, P.2
  • 78
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • Shields, R. L. et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277, 26733-26740 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 79
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T. et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278, 3466-3473 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1
  • 80
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S., Mimura, Y., Jefferis, R., Huber, R. & Sondermann, P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325, 979-989 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 81
    • 0024525036 scopus 로고
    • Interaction of human IgG chimeric antibodies with the human FcRI and FcRII receptors: Recruitements for antibody-mediated host cell-target cell interaction
    • Walker, M. R., Woof, J. M., Bruggemann, M., Jefferis, R. & Burton D. R. Interaction of human IgG chimeric antibodies with the human FcRI and FcRII receptors: recruitements for antibody-mediated host cell-target cell interaction. Mol. Immunol. 26, 403-411 (1989).
    • (1989) Mol. Immunol. , vol.26 , pp. 403-411
    • Walker, M.R.1    Woof, J.M.2    Bruggemann, M.3    Jefferis, R.4    Burton, D.R.5
  • 82
    • 0025020248 scopus 로고
    • Antibody: The flexible adaptor molecule
    • Burton, D. R. Antibody: the flexible adaptor molecule. Trends Biol. Sci. 15, 64-69 (1990).
    • (1990) Trends Biol. Sci. , vol.15 , pp. 64-69
    • Burton, D.R.1
  • 83
    • 0022905472 scopus 로고
    • Is IgM-like dislocation a common feature of antibody function?
    • Burton, D. R. Is IgM-like dislocation a common feature of antibody function? Immunol. Today 7, 165-167 (1986).
    • (1986) Immunol. Today , vol.7 , pp. 165-167
    • Burton, D.R.1
  • 84
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity IgE receptor within membrane domains
    • Field, K. A. Holowka D. & Baird B. Compartmentalized activation of the high affinity IgE receptor within membrane domains. J. Biol. Chem. 272, 4276-4280 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 85
    • 0033571650 scopus 로고    scopus 로고
    • γ-chain dependent recruitment of tyrosine kinases to membrane rafts by the human IgA receptor FcαR
    • Lang, M. L., Shen, L. & Wade, W. F. γ-chain dependent recruitment of tyrosine kinases to membrane rafts by the human IgA receptor FcαR. J. Immunol. 163, 5391-5398 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 5391-5398
    • Lang, M.L.1    Shen, L.2    Wade, W.F.3
  • 86
    • 0034744443 scopus 로고    scopus 로고
    • FcεRI as a paradigm for a lipid raft-dependent receptor in hematopoietic cells
    • Holowka, D. & Baird, B. FcεRI as a paradigm for a lipid raft-dependent receptor in hematopoietic cells. Semin. Immunol. 13, 99-105 (2001).
    • (2001) Semin. Immunol. , vol.13 , pp. 99-105
    • Holowka, D.1    Baird, B.2
  • 87
    • 0034744650 scopus 로고    scopus 로고
    • The clustered Fcγ receptor II is recruited to Lyn-containing membrane domains and undergoes phosphorylation in a cholesterol-dependent manner
    • Kwiatkowska, K. & Sobota, A. The clustered Fcγ receptor II is recruited to Lyn-containing membrane domains and undergoes phosphorylation in a cholesterol-dependent manner. Eur. J. Immunol. 31, 989-998 (2001).
    • (2001) Eur. J. Immunol. , vol.31 , pp. 989-998
    • Kwiatkowska, K.1    Sobota, A.2
  • 88
    • 0035889227 scopus 로고    scopus 로고
    • Association of FcγRII with low-density detergent-resistant membranes is important for crosslinking-dependent initiation of the tyrosine phosphorylation pathway and superoxide generation
    • Katsumata, O. et al. Association of FcγRII with low-density detergent-resistant membranes is important for crosslinking-dependent initiation of the tyrosine phosphorylation pathway and superoxide generation. J. Immunol. 167, 5814-5823 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 5814-5823
    • Katsumata, O.1
  • 89
    • 0036606184 scopus 로고    scopus 로고
    • IgA Fc receptor (FcαR) crosslinking recruits tyrosine kinases, phosphoinositide kinases and serine/threonine kinases to glycolipid rafts
    • Lang, M. L. et al. IgA Fc receptor (FcαR) crosslinking recruits tyrosine kinases, phosphoinositide kinases and serine/threonine kinases to glycolipid rafts. Biochem. J. 364, 517-525 (2002).
    • (2002) Biochem. J. , vol.364 , pp. 517-525
    • Lang, M.L.1
  • 91
    • 0035997958 scopus 로고    scopus 로고
    • Therapeutic monoclonal antibodies: Trends in development and approval in the US
    • Reichert, J. M. Therapeutic monoclonal antibodies: trends in development and approval in the US. Curr. Opin. Mol. Ther. 4, 110-118 (2002).
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , pp. 110-118
    • Reichert, J.M.1
  • 92
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • Brekke, O. H. & Sandlie, I. Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nature Rev. Drug Discov. 2, 52-62 (2003).
    • (2003) Nature Rev. Drug Discov. , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 93
    • 0037350545 scopus 로고    scopus 로고
    • Immunotherapy: Past, present and future
    • Waldmann, T. A. Immunotherapy: past, present and future. Nature Med. 9, 269-277 (2003).
    • (2003) Nature Med. , vol.9 , pp. 269-277
    • Waldmann, T.A.1
  • 94
    • 0036020617 scopus 로고    scopus 로고
    • Engineering antibodies for therapy
    • Presta, L. G. Engineering antibodies for therapy. Curr. Pharmaceut. Biotechnol. 3, 237-256 (2002).
    • (2002) Curr. Pharmaceut. Biotechnol. , vol.3 , pp. 237-256
    • Presta, L.G.1
  • 95
    • 0036467723 scopus 로고    scopus 로고
    • Recombinant immunoglobulin A: Powerful tools for fundamental and applied research
    • Corthésy, B. Recombinant immunoglobulin A: powerful tools for fundamental and applied research. Trends Biotechnol. 20, 65-71 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 65-71
    • Corthésy, B.1
  • 96
    • 0001500510 scopus 로고
    • Three-dimensional structure of an intact human immunoglobulin
    • Silverton, E. W., Navia, M. A. & Davies, D. R. Three-dimensional structure of an intact human immunoglobulin. Proc. Natl Acad. Sci. USA 74, 5140-5144 (1977).
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5140-5144
    • Silverton, E.W.1    Navia, M.A.2    Davies, D.R.3
  • 97
    • 0027154092 scopus 로고
    • Three-dimensional structure of a human immunoglobulin with a hinge deletion
    • Guddat, L. W., Herron J. N. & Edmundson, A. B. Three-dimensional structure of a human immunoglobulin with a hinge deletion. Proc. Natl Acad. Sci. USA 90, 4271-4275 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4271-4275
    • Guddat, L.W.1    Herron, J.N.2    Edmundson, A.B.3


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