메뉴 건너뛰기




Volumn 2, Issue , 2016, Pages 15-22

IgG Structure and Function

Author keywords

Antibody; Antigen; Complement; Constant domain; Effector function; Fc R; Glycoprotein; Humoral immunity; Immunoglobulin fold; Subclass; Variable domain

Indexed keywords


EID: 84957711865     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374279-7.05002-5     Document Type: Chapter
Times cited : (16)

References (71)
  • 2
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B., Lesk A.M., Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 1997, 273:927-948.
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 5
    • 0018654090 scopus 로고
    • Three-dimensional structure of immunoglobulins
    • Amzel L.M., Poljak R.J. Three-dimensional structure of immunoglobulins. Annu. Rev. Biochem. 1979, 48:961-997.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 961-997
    • Amzel, L.M.1    Poljak, R.J.2
  • 6
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 7
    • 0014022299 scopus 로고
    • The transmission of immunity from mother to young and the catabolism of immunoglobulins
    • Brambell F.W. The transmission of immunity from mother to young and the catabolism of immunoglobulins. Lancet 1966, 2:1087-1093.
    • (1966) Lancet , vol.2 , pp. 1087-1093
    • Brambell, F.W.1
  • 8
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
    • Bransteitter R., Pham P., Scharff M.D., Goodman M.F. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:4102-4107.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4102-4107
    • Bransteitter, R.1    Pham, P.2    Scharff, M.D.3    Goodman, M.F.4
  • 9
    • 0017280292 scopus 로고
    • A modification of Jerne's theory of antibody production using the concept of clonal selection
    • Burnet F.M. A modification of Jerne's theory of antibody production using the concept of clonal selection. CA Cancer J. Clin. 1976, 26:119-121.
    • (1976) CA Cancer J. Clin. , vol.26 , pp. 119-121
    • Burnet, F.M.1
  • 10
    • 33749528353 scopus 로고    scopus 로고
    • Antibody repertoire development in fetal and neonatal piglets. XVII. IgG subclass transcription revisited with emphasis on new IgG3
    • Butler J.E., Wertz N. Antibody repertoire development in fetal and neonatal piglets. XVII. IgG subclass transcription revisited with emphasis on new IgG3. J. Immunol. 2006, 177:5480-5489.
    • (2006) J. Immunol. , vol.177 , pp. 5480-5489
    • Butler, J.E.1    Wertz, N.2
  • 12
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter P.J. Potent antibody therapeutics by design. Nat. Rev. Immunol. 2006, 6:343-357.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 15
    • 0021216208 scopus 로고
    • Insertion of N regions into heavy-chain genes is correlated with expression of terminal deoxytransferase in B cells
    • Desiderio S.V., Yancopoulos G.D., Paskind M., Thomas E., Boss M.A., Landau N., Alt F.W., Baltimore D. Insertion of N regions into heavy-chain genes is correlated with expression of terminal deoxytransferase in B cells. Nature 1984, 311:752-755.
    • (1984) Nature , vol.311 , pp. 752-755
    • Desiderio, S.V.1    Yancopoulos, G.D.2    Paskind, M.3    Thomas, E.4    Boss, M.A.5    Landau, N.6    Alt, F.W.7    Baltimore, D.8
  • 19
    • 0033519426 scopus 로고    scopus 로고
    • Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry
    • Ghirlando R., Lund J., Goodall M., Jefferis R. Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry. Immunol. Lett. 1999, 68:47-52.
    • (1999) Immunol. Lett. , vol.68 , pp. 47-52
    • Ghirlando, R.1    Lund, J.2    Goodall, M.3    Jefferis, R.4
  • 20
    • 0020567861 scopus 로고
    • A tissue-specific transcription enhancer element is located in the major intron of a rearranged immunoglobulin heavy chain gene
    • Gillies S.D., Morrison S.L., Oi V.T., Tonegawa S. A tissue-specific transcription enhancer element is located in the major intron of a rearranged immunoglobulin heavy chain gene. Cell 1983, 33:717-728.
    • (1983) Cell , vol.33 , pp. 717-728
    • Gillies, S.D.1    Morrison, S.L.2    Oi, V.T.3    Tonegawa, S.4
  • 21
    • 0023530681 scopus 로고
    • Human IgG subclass measurements in the clinical laboratory
    • Hamilton R.G. Human IgG subclass measurements in the clinical laboratory. Clin. Chem. 1987, 33:1707-1725.
    • (1987) Clin. Chem. , vol.33 , pp. 1707-1725
    • Hamilton, R.G.1
  • 22
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 1994, 238:528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 23
    • 0031017896 scopus 로고    scopus 로고
    • Refined structure of an intact IgG2a monoclonal antibody
    • Harris L.J., Larson S.B., Hasel K.W., Mcpherson A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 1997, 36:1581-1597.
    • (1997) Biochemistry , vol.36 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    Mcpherson, A.4
  • 24
    • 0026505119 scopus 로고
    • Regulation of C gamma 3 expression. Role of switch in the allotype-associated variation of human serum IgG3 levels
    • Hassan M.S., Islam K.B., Hammarstrom L., Smith C.I. Regulation of C gamma 3 expression. Role of switch in the allotype-associated variation of human serum IgG3 levels. J. Immunol. 1992, 148:2555-2562.
    • (1992) J. Immunol. , vol.148 , pp. 2555-2562
    • Hassan, M.S.1    Islam, K.B.2    Hammarstrom, L.3    Smith, C.I.4
  • 25
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F., Hogan S., Latypov R.F., Narhi L.O., Razinkov V.I. High throughput thermostability screening of monoclonal antibody formulations. J. Pharm. Sci. 2010, 99:1707-1720.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 26
    • 0035827172 scopus 로고    scopus 로고
    • Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool
    • Honegger A., Pluckthun A. Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool. J. Mol. Biol. 2001, 309:657-670.
    • (2001) J. Mol. Biol. , vol.309 , pp. 657-670
    • Honegger, A.1    Pluckthun, A.2
  • 27
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu R.M., Vlasak J., Price C., Kirchmeier M. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J. Pharm. Sci. 2008, 97:1414-1426.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 28
    • 84892369713 scopus 로고    scopus 로고
    • Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress
    • Ito T., Tsumoto K. Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress. Protein Sci. 2013, 22:1542-1551.
    • (2013) Protein Sci. , vol.22 , pp. 1542-1551
    • Ito, T.1    Tsumoto, K.2
  • 29
    • 0033971477 scopus 로고    scopus 로고
    • Kabat database and its applications: 30 years after the first variability plot
    • Johnson G., Wu T.T. Kabat database and its applications: 30 years after the first variability plot. Nucleic Acids Res. 2000, 28:214-218.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 214-218
    • Johnson, G.1    Wu, T.T.2
  • 30
    • 0029891262 scopus 로고    scopus 로고
    • The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor
    • Junghans R.P., Anderson C.L. The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:5512-5516.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 31
    • 0014252693 scopus 로고
    • Unique features of the variable regions of Bence Jones proteins and their possible relation to antibody complementarity
    • Kabat E.A. Unique features of the variable regions of Bence Jones proteins and their possible relation to antibody complementarity. Proc. Natl. Acad. Sci. U.S.A. 1968, 59:613-619.
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 613-619
    • Kabat, E.A.1
  • 33
    • 0029807629 scopus 로고    scopus 로고
    • B cells are exquisitely sensitive to central tolerance and receptor editing induced by ultralow affinity, membrane-bound antigen
    • Lang J., Jackson M., Teyton L., Brunmark A., Kane K., Nemazee D. B cells are exquisitely sensitive to central tolerance and receptor editing induced by ultralow affinity, membrane-bound antigen. J. Exp. Med. 1996, 184:1685-1697.
    • (1996) J. Exp. Med. , vol.184 , pp. 1685-1697
    • Lang, J.1    Jackson, M.2    Teyton, L.3    Brunmark, A.4    Kane, K.5    Nemazee, D.6
  • 34
    • 84862945390 scopus 로고    scopus 로고
    • Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc
    • Latypov R.F., Hogan S., Lau H., Gadgil H., Liu D. Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc. J. Biol. Chem. 2012, 287:1381-1396.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1381-1396
    • Latypov, R.F.1    Hogan, S.2    Lau, H.3    Gadgil, H.4    Liu, D.5
  • 35
    • 0000590741 scopus 로고
    • Genes and antibodies
    • Lederberg J. Genes and antibodies. Science 1959, 129:1649-1653.
    • (1959) Science , vol.129 , pp. 1649-1653
    • Lederberg, J.1
  • 36
    • 0036823113 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics database: a high-quality information system for comparative immunogenetics and immunology
    • Lefranc M.P. IMGT, the international ImMunoGeneTics database: a high-quality information system for comparative immunogenetics and immunology. Dev. Comp. Immunol. 2002, 26:697-705.
    • (2002) Dev. Comp. Immunol. , vol.26 , pp. 697-705
    • Lefranc, M.P.1
  • 37
    • 84925883851 scopus 로고    scopus 로고
    • Immunoinformatics of the V, C, and G domains: IMGT(R) definitive system for IG, TR and IgSF, MH, and MhSF
    • Lefranc M.P. Immunoinformatics of the V, C, and G domains: IMGT(R) definitive system for IG, TR and IgSF, MH, and MhSF. Methods Mol. Biol. 2014, 1184:59-107.
    • (2014) Methods Mol. Biol. , vol.1184 , pp. 59-107
    • Lefranc, M.P.1
  • 40
    • 84872518803 scopus 로고    scopus 로고
    • Of mice and men: the need for humanized mouse models to study human IgG activity in vivo
    • Lux A., Nimmerjahn F. Of mice and men: the need for humanized mouse models to study human IgG activity in vivo. J. Clin. Immunol. 2013, 33(Suppl. 1):S4-S8.
    • (2013) J. Clin. Immunol. , vol.33 , pp. S4-S8
    • Lux, A.1    Nimmerjahn, F.2
  • 42
    • 84930822871 scopus 로고    scopus 로고
    • FcgammaR dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities
    • Nimmerjahn F., Gordan S., Lux A. FcgammaR dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities. Trends Immunol. 2015, 36:325-336.
    • (2015) Trends Immunol. , vol.36 , pp. 325-336
    • Nimmerjahn, F.1    Gordan, S.2    Lux, A.3
  • 43
    • 28544449847 scopus 로고    scopus 로고
    • Divergent immunoglobulin G subclass activity through selective Fc receptor binding
    • Nimmerjahn F., Ravetch J.V. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science 2005, 310:1510-1512.
    • (2005) Science , vol.310 , pp. 1510-1512
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 44
    • 0000735306 scopus 로고
    • Antibody production by single cells
    • Nossal G.J., Lederberg J. Antibody production by single cells. Nature 1958, 181:1419-1420.
    • (1958) Nature , vol.181 , pp. 1419-1420
    • Nossal, G.J.1    Lederberg, J.2
  • 46
    • 33947445379 scopus 로고
    • A theory of the structure and process of formation of antibodies
    • Pauling L. A theory of the structure and process of formation of antibodies. J. Am. Chem. Soc. 1940, 62:2643-2657.
    • (1940) J. Am. Chem. Soc. , vol.62 , pp. 2643-2657
    • Pauling, L.1
  • 48
    • 70449276523 scopus 로고
    • The hydrolysis of rabbit y-globulin and antibodies with crystalline papain
    • Porter R.R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem. J. 1959, 73:119-126.
    • (1959) Biochem. J. , vol.73 , pp. 119-126
    • Porter, R.R.1
  • 53
    • 36849001338 scopus 로고    scopus 로고
    • Isotype selection in antibody engineering
    • Salfeld J.G. Isotype selection in antibody engineering. Nat. Biotechnol. 2007, 25:1369-1372.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1369-1372
    • Salfeld, J.G.1
  • 54
    • 0015840644 scopus 로고
    • Structure of a lambda-type Bence-Jones protein at 3.5-Å resolution
    • Schiffer M., Girling R.L., Ely K.R., Edmundson A.B. Structure of a lambda-type Bence-Jones protein at 3.5-Å resolution. Biochemistry 1973, 12:4620-4631.
    • (1973) Biochemistry , vol.12 , pp. 4620-4631
    • Schiffer, M.1    Girling, R.L.2    Ely, K.R.3    Edmundson, A.B.4
  • 55
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields R.L., Lai J., Keck R., O'connell L.Y., Hong K., Meng Y.G., Weikert S.H., Presta L.G. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 2002, 277:26733-26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 56
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields R.L., Namenuk A.K., Hong K., Meng Y.G., Rae J., Briggs J., Xie D., Lai J., Stadlen A., Li B., Fox J.A., Presta L.G. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J. Biol. Chem. 2001, 276:6591-6604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10    Fox, J.A.11    Presta, L.G.12
  • 57
    • 0037025895 scopus 로고    scopus 로고
    • Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: functional expression of FcRn in the mammalian lung
    • Spiekermann G.M., Finn P.W., Ward E.S., Dumont J., Dickinson B.L., Blumberg R.S., Lencer W.I. Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: functional expression of FcRn in the mammalian lung. J. Exp. Med. 2002, 196:303-310.
    • (2002) J. Exp. Med. , vol.196 , pp. 303-310
    • Spiekermann, G.M.1    Finn, P.W.2    Ward, E.S.3    Dumont, J.4    Dickinson, B.L.5    Blumberg, R.S.6    Lencer, W.I.7
  • 58
    • 84864502516 scopus 로고    scopus 로고
    • Russell body inducing threshold depends on the variable domain sequences of individual human IgG clones and the cellular protein homeostasis
    • Stoops J., Byrd S., Hasegawa H. Russell body inducing threshold depends on the variable domain sequences of individual human IgG clones and the cellular protein homeostasis. Biochim. Biophys. Acta 2012, 1823:1643-1657.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1643-1657
    • Stoops, J.1    Byrd, S.2    Hasegawa, H.3
  • 59
    • 37049242573 scopus 로고
    • Immunological specificity, unique combinations of selected natural globulins provide an alternative to the classical concept
    • Talmage D.W. Immunological specificity, unique combinations of selected natural globulins provide an alternative to the classical concept. Science 1959, 129:1643-1648.
    • (1959) Science , vol.129 , pp. 1643-1648
    • Talmage, D.W.1
  • 60
    • 0036091560 scopus 로고    scopus 로고
    • Distinct and opposite diversifying activities of terminal transferase splice variants
    • Thai T.H., Purugganan M.M., Roth D.B., Kearney J.F. Distinct and opposite diversifying activities of terminal transferase splice variants. Nat. Immunol. 2002, 3:457-462.
    • (2002) Nat. Immunol. , vol.3 , pp. 457-462
    • Thai, T.H.1    Purugganan, M.M.2    Roth, D.B.3    Kearney, J.F.4
  • 61
    • 53549108576 scopus 로고    scopus 로고
    • Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus
    • Thomson C.A., Bryson S., Mclean G.R., Creagh A.L., Pai E.F., Schrader J.W. Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus. EMBO J. 2008, 27:2592-2602.
    • (2008) EMBO J. , vol.27 , pp. 2592-2602
    • Thomson, C.A.1    Bryson, S.2    Mclean, G.R.3    Creagh, A.L.4    Pai, E.F.5    Schrader, J.W.6
  • 62
    • 0027478391 scopus 로고
    • Receptor editing in self-reactive bone marrow B cells
    • Tiegs S.L., Russell D.M., Nemazee D. Receptor editing in self-reactive bone marrow B cells. J. Exp. Med. 1993, 177:1009-1020.
    • (1993) J. Exp. Med. , vol.177 , pp. 1009-1020
    • Tiegs, S.L.1    Russell, D.M.2    Nemazee, D.3
  • 64
    • 84918825382 scopus 로고    scopus 로고
    • IgG subclasses and allotypes: from structure to effector functions
    • Vidarsson G., Dekkers G., Rispens T. IgG subclasses and allotypes: from structure to effector functions. Front. Immunol. 2014, 5:520.
    • (2014) Front. Immunol. , vol.5 , pp. 520
    • Vidarsson, G.1    Dekkers, G.2    Rispens, T.3
  • 67
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure
    • Wright A., Tao M.H., Kabat E.A., Morrison S.L. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J. 1991, 10:2717-2723.
    • (1991) EMBO J. , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3    Morrison, S.L.4
  • 68
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu T.T., Kabat E.A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J. Exp. Med. 1970, 132:211-250.
    • (1970) J. Exp. Med. , vol.132 , pp. 211-250
    • Wu, T.T.1    Kabat, E.A.2
  • 70
    • 84904460487 scopus 로고    scopus 로고
    • Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction
    • Zhu K., Day T., Warshaviak D., Murrett C., Friesner R., Pearlman D. Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction. Proteins 2014, 82:1646-1655.
    • (2014) Proteins , vol.82 , pp. 1646-1655
    • Zhu, K.1    Day, T.2    Warshaviak, D.3    Murrett, C.4    Friesner, R.5    Pearlman, D.6
  • 71
    • 85043247006 scopus 로고    scopus 로고
    • IMGT(c), the International Immunogenetics Information System.
    • - IMGT(c), the International Immunogenetics Information System. http://www.imgt.org/.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.