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Volumn 22, Issue 12, 2015, Pages 953-958

Structure of full-length human anti-PD1 therapeutic IgG4 antibody pembrolizumab

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C1Q; FC RECEPTOR; GLYCAN; HYDROGEN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4; OXYGEN; PEMBROLIZUMAB; ANTINEOPLASTIC AGENT; MONOCLONAL ANTIBODY; PDCD1 PROTEIN, HUMAN; PROGRAMMED DEATH 1 RECEPTOR;

EID: 84949533006     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3129     Document Type: Article
Times cited : (198)

References (40)
  • 1
    • 84255197842 scopus 로고    scopus 로고
    • Cancer immunotherapy comes of age
    • Mellman I., Coukos G., & Dranoff G. Cancer immunotherapy comes of age. Nature. 480, 480-489 (2011
    • (2011) Nature , vol.480 , pp. 480-489
    • Mellman, I.1    Coukos, G.2    Dranoff, G.3
  • 2
    • 84879625854 scopus 로고    scopus 로고
    • New checkpoint inhibitors ride the immunotherapy tsunami
    • Mullard A. New checkpoint inhibitors ride the immunotherapy tsunami. Nat. Rev. Drug Discov. 12, 489-492 (2013
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 489-492
    • Mullard, A.1
  • 4
    • 34548694517 scopus 로고    scopus 로고
    • Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange
    • van der Neut Kolfschoten M., et al. Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange. Science. 317, 1554-1557 (2007
    • (2007) Science , vol.317 , pp. 1554-1557
    • Van Der Neut Kolfschoten, M.1
  • 5
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for Fc?R: Current models
    • Jefferis R., & Lund J. Interaction sites on human IgG-Fc for Fc?R: current models. Immunol. Lett. 82, 57-65 (2002
    • (2002) Immunol. Lett , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 6
    • 84865677743 scopus 로고    scopus 로고
    • Isotype and glycoform selection for antibody therapeutics
    • Jefferis R. Isotype and glycoform selection for antibody therapeutics. Arch. Biochem. Biophys. 526, 159-166 (2012
    • (2012) Arch. Biochem. Biophys , vol.526 , pp. 159-166
    • Jefferis, R.1
  • 7
    • 0024635830 scopus 로고
    • The primary structure of crystallizable monoclonal immunoglobulin IgG1 Kol II Amino acid sequence of the L-chain, gamma-Type, subgroup i
    • Kratzin H.D., et al. The primary structure of crystallizable monoclonal immunoglobulin IgG1 Kol. II. Amino acid sequence of the L-chain, gamma-Type, subgroup I. Biol. Chem. Hoppe Seyler. 370, 263-272 (1989
    • (1989) Biol. Chem. Hoppe Seyler , vol.370 , pp. 263-272
    • Kratzin, H.D.1
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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. 36, 1581-1597 (1997
    • (1997) Biochemistry , vol.36 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    McPherson, A.4
  • 12
    • 84892525003 scopus 로고    scopus 로고
    • Structural determinants of unique properties of human IgG4-Fc
    • Davies A.M., et al. Structural determinants of unique properties of human IgG4-Fc. J. Mol. Biol. 426, 630-644 (2014
    • (2014) J. Mol. Biol , vol.426 , pp. 630-644
    • Davies, A.M.1
  • 13
    • 0036010538 scopus 로고    scopus 로고
    • Recognitions of immunoglobulins by Fc receptors
    • Radaev S., & Sun P. Recognitions of immunoglobulins by Fc? receptors. Mol. Immunol. 38, 1073-1083 (2002
    • (2002) Mol. Immunol , vol.38 , pp. 1073-1083
    • Radaev, S.1    Sun, P.2
  • 14
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fc receptors and their polymorphic variants for human IgG subclasses
    • Bruhns P., et al. Specificity and affinity of human Fc? receptors and their polymorphic variants for human IgG subclasses. Blood. 113, 3716-3725 (2009
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1
  • 15
    • 84859567109 scopus 로고    scopus 로고
    • Atomic resolution model of the antibody Fc interaction with the complement C1q component
    • Schneider S., & Zacharias M. Atomic resolution model of the antibody Fc interaction with the complement C1q component. Mol. Immunol. 51, 66-72 (2012
    • (2012) Mol. Immunol , vol.51 , pp. 66-72
    • Schneider, S.1    Zacharias, M.2
  • 16
    • 0000867858 scopus 로고    scopus 로고
    • Single transition-To-single transition polarization transfer (ST2-PT) in [15N,1H] -TROSY
    • Pervushin K.V., Wider G., & Wüthrich K. Single transition-To-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY. J. Biomol. NMR. 12, 345-348 (1998
    • (1998) J. Biomol. NMR , vol.12 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wüthrich, K.3
  • 17
    • 84926638538 scopus 로고    scopus 로고
    • Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance
    • Arbogast L.W., Brinson R.G., & Marino J.P. Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance. Anal. Chem. 87, 3556-3561 (2015
    • (2015) Anal. Chem , vol.87 , pp. 3556-3561
    • Arbogast, L.W.1    Brinson, R.G.2    Marino, J.P.3
  • 18
    • 84940928369 scopus 로고    scopus 로고
    • In-depth analysis of subclass-specific conformational preferences of IgG antibodies
    • Tian X., et al. In-depth analysis of subclass-specific conformational preferences of IgG antibodies. IUCrJ. 2, 9-18 (2015
    • (2015) IUCrJ , vol.2 , pp. 9-18
    • Tian, X.1
  • 19
    • 0027216004 scopus 로고
    • A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody
    • Angal S., et al. A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody. Mol. Immunol. 30, 105-108 (1993
    • (1993) Mol. Immunol , vol.30 , pp. 105-108
    • Angal, S.1
  • 20
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structures
    • Richardson J.S. The anatomy and taxonomy of protein structures. Adv. Protein Chem. 34, 167-339 (1981
    • (1981) Adv. Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 21
    • 84886937973 scopus 로고    scopus 로고
    • Profiling formulated monoclonal antibodies by 1H NMR spectroscopy
    • Poppe L., et al. Profiling formulated monoclonal antibodies by 1H NMR spectroscopy. Anal. Chem. 85, 9623-9629 (2013
    • (2013) Anal. Chem , vol.85 , pp. 9623-9629
    • Poppe, L.1
  • 22
    • 84905386771 scopus 로고    scopus 로고
    • The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: Implications for functional activity
    • Rayner L.E., et al. The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: implications for functional activity. J. Biol. Chem. 289, 20740-20756 (2014
    • (2014) J. Biol. Chem , vol.289 , pp. 20740-20756
    • Rayner, L.E.1
  • 23
    • 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., et al. 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. 276, 6591-6604 (2001
    • (2001) J. Biol. Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1
  • 24
    • 0034691322 scopus 로고    scopus 로고
    • The 3 2-Å crystal structure of the human IgG1 Fc fragment-Fc?RIII complex
    • Sondermann P., Huber R., Oosthuizen V., & Jacob U. The 3.2-? crystal structure of the human IgG1 Fc fragment-Fc?RIII complex. Nature. 406, 267-273 (2000
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 26
    • 0027213573 scopus 로고
    • Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation
    • Tao M.H., Smith R.I., & Morrison S.L. Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation. J. Exp. Med. 178, 661-667 (1993
    • (1993) J. Exp. Med , vol.178 , pp. 661-667
    • Tao, M.H.1    Smith, R.I.2    Morrison, S.L.3
  • 27
    • 84896265417 scopus 로고    scopus 로고
    • Structural insights into neonatal Fc receptor-based recycling mechanisms
    • Oganesyan V., et al. Structural insights into neonatal Fc receptor-based recycling mechanisms. J. Biol. Chem. 289, 7812-7824 (2014
    • (2014) J. Biol. Chem , vol.289 , pp. 7812-7824
    • Oganesyan, V.1
  • 28
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8 Å of an FcRn/hetrodimeric Fc complex: Mechanism of pH-dependent binding
    • Martin W.L., West A.P., Gan L., & Bjorkman P.J. Crystal structure at 2.8 Å of an FcRn/hetrodimeric 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, A.P.2    Gan, L.3    Bjorkman, P.J.4
  • 29
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • West A.P., & Bjorkman P.J. Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor. Biochemistry. 39, 9698-9708 (2000
    • (2000) Biochemistry , vol.39 , pp. 9698-9708
    • West, A.P.1    Bjorkman, P.J.2
  • 30
    • 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. 25, 21-50 (2007
    • (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
  • 31
    • 84905090765 scopus 로고    scopus 로고
    • Fc glycan-modulated immunoglobulin G effector functions
    • Quast I., & Lünemann J.D. Fc glycan-modulated immunoglobulin G effector functions. J. Clin. Immunol. 34, S51-S55 (2014
    • (2014) J. Clin. Immunol , vol.34 , pp. S51-S55
    • Quast, I.1    Lünemann, J.D.2
  • 32
    • 80053578013 scopus 로고    scopus 로고
    • Impact of differential glycosylation on IgG activity
    • Lux A., & Nimmerjahn F. Impact of differential glycosylation on IgG activity. Adv. Exp. Med. Biol. 780, 113-124 (2011
    • (2011) Adv. Exp. Med. Biol , vol.780 , pp. 113-124
    • Lux, A.1    Nimmerjahn, F.2
  • 33
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • Barb A.W., & Prestegard J.H. NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nat. Chem. Biol. 7, 147-153 (2011
    • (2011) Nat. Chem. Biol , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 34
    • 84954390191 scopus 로고    scopus 로고
    • Comprehensive analysis of the therapeutic IgG4 antibody pembrolizumab: Hinge modification blocks half molecule exchange in vitro and in vivo
    • 26 August
    • Yang X., et al. Comprehensive analysis of the therapeutic IgG4 antibody pembrolizumab: hinge modification blocks half molecule exchange in vitro and in vivo. J. Pharm. Sci. doi:10.1002/jps.24620 (26 August 2015
    • (2015) J. Pharm. Sci
    • Yang, X.1
  • 35
    • 79953733151 scopus 로고    scopus 로고
    • Data processing and analysis with the autoPROC toolbox
    • Vonrhein C., et al. Data processing and analysis with the autoPROC toolbox. Acta Crystallogr. D Biol. Crystallogr. 67, 293-302 (2011
    • (2011) Acta Crystallogr. D Biol. Crystallogr , vol.67 , pp. 293-302
    • Vonrhein, C.1
  • 36
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy A.J., et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N4
    • Collaborative Computational Project N4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 40
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., & Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133 (2001
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3


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