메뉴 건너뛰기




Volumn 25, Issue 6, 2017, Pages 878-889.e5

Fcab-HER2 Interaction: a Ménage à Trois. Lessons from X-Ray and Solution Studies

Author keywords

binding stoichiometry; ErbB2; Fcab; Fcab HER2 structure; fluorescence correlation spectroscopy; HER2; IgG1 Fc; X ray crystallography

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; HOMODIMER; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; ERBB2 PROTEIN, HUMAN; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; PERTUZUMAB; TRASTUZUMAB;

EID: 85019346516     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2017.04.014     Document Type: Article
Times cited : (26)

References (56)
  • 1
    • 0001314221 scopus 로고
    • The hemoglobin system: VI. The oxygen dissociation curve of hemoglobin
    • Adair, G.S., Bock, A.V., Field, H., The hemoglobin system: VI. The oxygen dissociation curve of hemoglobin. J. Biol. Chem. 63 (1925), 529–545.
    • (1925) J. Biol. Chem. , vol.63 , pp. 529-545
    • Adair, G.S.1    Bock, A.V.2    Field, H.3
  • 5
    • 84877700145 scopus 로고    scopus 로고
    • Structural and thermodynamic insights into the recognition of native proteins by anti-peptide antibodies
    • Armstrong, A., Hildreth, J.E., Amzel, L.M., Structural and thermodynamic insights into the recognition of native proteins by anti-peptide antibodies. J. Mol. Biol. 425 (2013), 2027–2038.
    • (2013) J. Mol. Biol. , vol.425 , pp. 2027-2038
    • Armstrong, A.1    Hildreth, J.E.2    Amzel, L.M.3
  • 6
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • Borrok, M.J., Jung, S.T., Kang, T.H., Monzingo, A.F., Georgiou, G., Revisiting the role of glycosylation in the structure of human IgG Fc. ACS Chem. Biol. 7 (2012), 1596–1602.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1596-1602
    • Borrok, M.J.1    Jung, S.T.2    Kang, T.H.3    Monzingo, A.F.4    Georgiou, G.5
  • 7
    • 27244461099 scopus 로고    scopus 로고
    • The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand
    • Bouyain, S., Longo, P.A., Li, S., Ferguson, K.M., Leahy, D.J., The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc. Natl. Acad. Sci. USA 102 (2005), 15024–15029.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15024-15029
    • Bouyain, S.1    Longo, P.A.2    Li, S.3    Ferguson, K.M.4    Leahy, D.J.5
  • 9
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho, H.S., Mason, K., Ramyar, K.X., Stanley, A.M., Gabelli, S.B., Denney, D.W. Jr., Leahy, D.J., Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421 (2003), 756–760.
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney, D.W.6    Leahy, D.J.7
  • 10
    • 33845241063 scopus 로고    scopus 로고
    • Time, the forgotten dimension of ligand binding teaching
    • Corzo, J., Time, the forgotten dimension of ligand binding teaching. Biochem. Mol. Biol. Educ. 34 (2006), 413–416.
    • (2006) Biochem. Mol. Biol. Educ. , vol.34 , pp. 413-416
    • Corzo, J.1
  • 11
  • 12
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., Perret, S., Kamen, A., High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res., 30, 2002, E9.
    • (2002) Nucleic Acids Res. , vol.30 , pp. E9
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 13
    • 0023803794 scopus 로고
    • The physical basis for induction of protein-reactive antipeptide antibodies
    • Dyson, H.J., Lerner, R.A., Wright, P.E., The physical basis for induction of protein-reactive antipeptide antibodies. Annu. Rev. Biophys. Biophys. Chem. 17 (1988), 305–324.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 305-324
    • Dyson, H.J.1    Lerner, R.A.2    Wright, P.E.3
  • 17
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family: sequence analysis and 3D structure comparisons
    • Halaby, D.M., Poupon, A., Mornon, J., The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Protein Eng. 12 (1999), 563–571.
    • (1999) Protein Eng. , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.3
  • 18
    • 0028846780 scopus 로고
    • Crystallization of intact monoclonal antibodies
    • Harris, L.J., Skaletsky, E., McPherson, A., Crystallization of intact monoclonal antibodies. Proteins 23 (1995), 285–289.
    • (1995) Proteins , vol.23 , pp. 285-289
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 19
    • 84885001319 scopus 로고    scopus 로고
    • Stability assessment on a library scale: a rapid method for the evaluation of the commutability and insertion of residues in C-terminal loops of the CH3 domains of IgG1-Fc
    • Hasenhindl, C., Traxlmayr, M.W., Wozniak-Knopp, G., Jones, P.C., Stadlmayr, G., Ruker, F., Obinger, C., Stability assessment on a library scale: a rapid method for the evaluation of the commutability and insertion of residues in C-terminal loops of the CH3 domains of IgG1-Fc. Protein Eng. Des. Sel. 26 (2013), 675–682.
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 675-682
    • Hasenhindl, C.1    Traxlmayr, M.W.2    Wozniak-Knopp, G.3    Jones, P.C.4    Stadlmayr, G.5    Ruker, F.6    Obinger, C.7
  • 20
    • 84957991319 scopus 로고    scopus 로고
    • N-glycosylation heterogeneity and the influence on structure, function and pharmacokinetics of monoclonal antibodies and Fc fusion proteins
    • Higel, F., Seidl, A., Sorgel, F., Friess, W., N-glycosylation heterogeneity and the influence on structure, function and pharmacokinetics of monoclonal antibodies and Fc fusion proteins. Eur. J. Pharm. Biopharm. 100 (2016), 94–100.
    • (2016) Eur. J. Pharm. Biopharm. , vol.100 , pp. 94-100
    • Higel, F.1    Seidl, A.2    Sorgel, F.3    Friess, W.4
  • 21
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger, P., Hudson, P.J., Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 23 (2005), 1126–1136.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 23
    • 78049403279 scopus 로고    scopus 로고
    • Ligand binding assays at equilibrium: validation and interpretation
    • Hulme, E.C., Trevethick, M.A., Ligand binding assays at equilibrium: validation and interpretation. Br. J. Pharmacol. 161 (2010), 1219–1237.
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1219-1237
    • Hulme, E.C.1    Trevethick, M.A.2
  • 26
    • 84922361077 scopus 로고    scopus 로고
    • The PDB_REDO server for macromolecular structure model optimization
    • Joosten, R.P., Long, F., Murshudov, G.N., Perrakis, A., The PDB_REDO server for macromolecular structure model optimization. IUCrJ 1 (2014), 213–220.
    • (2014) IUCrJ , vol.1 , pp. 213-220
    • Joosten, R.P.1    Long, F.2    Murshudov, G.N.3    Perrakis, A.4
  • 28
    • 84865691682 scopus 로고    scopus 로고
    • Correlation between CD16a binding and immuno effector functionality of an antigen specific immunoglobulin Fc fragment (Fcab)
    • Kainer, M., Antes, B., Wiederkum, S., Wozniak-Knopp, G., Bauer, A., Ruker, F., Woisetschläger, M., Correlation between CD16a binding and immuno effector functionality of an antigen specific immunoglobulin Fc fragment (Fcab). Arch. Biochem. Biophys. 526 (2012), 154–158.
    • (2012) Arch. Biochem. Biophys. , vol.526 , pp. 154-158
    • Kainer, M.1    Antes, B.2    Wiederkum, S.3    Wozniak-Knopp, G.4    Bauer, A.5    Ruker, F.6    Woisetschläger, M.7
  • 29
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P.A., Diederichs, K., Linking crystallographic model and data quality. Science 336 (2012), 1030–1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 30
    • 0001180450 scopus 로고
    • The application of the law of mass action to binding by proteins; interactions with calcium
    • Klotz, I.M., The application of the law of mass action to binding by proteins; interactions with calcium. Arch. Biochem. 9 (1946), 109–117.
    • (1946) Arch. Biochem. , vol.9 , pp. 109-117
    • Klotz, I.M.1
  • 31
    • 0346098059 scopus 로고    scopus 로고
    • Ligand-receptor complexes: origin and development of the concept
    • Klotz, I.M., Ligand-receptor complexes: origin and development of the concept. J. Biol. Chem. 279 (2004), 1–12.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1-12
    • Klotz, I.M.1
  • 32
    • 84930714069 scopus 로고    scopus 로고
    • A structural perspective on the regulation of the epidermal growth factor receptor
    • Kovacs, E., Zorn, J.A., Huang, Y., Barros, T., Kuriyan, J., A structural perspective on the regulation of the epidermal growth factor receptor. Annu. Rev. Biochem. 84 (2015), 739–764.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 739-764
    • Kovacs, E.1    Zorn, J.A.2    Huang, Y.3    Barros, T.4    Kuriyan, J.5
  • 33
    • 70149086034 scopus 로고    scopus 로고
    • Engineered therapeutic antibodies with improved effector functions
    • Kubota, T., Niwa, R., Satoh, M., Akinaga, S., Shitara, K., Hanai, N., Engineered therapeutic antibodies with improved effector functions. Cancer Sci. 100 (2009), 1566–1572.
    • (2009) Cancer Sci. , vol.100 , pp. 1566-1572
    • Kubota, T.1    Niwa, R.2    Satoh, M.3    Akinaga, S.4    Shitara, K.5    Hanai, N.6
  • 34
    • 0033662957 scopus 로고    scopus 로고
    • A mammalian expression vector for expression and purification of secreted proteins for structural studies
    • Leahy, D.J., Dann, C.E. 3rd, Longo, P., Perman, B., Ramyar, K.X., A mammalian expression vector for expression and purification of secreted proteins for structural studies. Protein Expr. Purif. 20 (2000), 500–506.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 500-506
    • Leahy, D.J.1    Dann, C.E.2    Longo, P.3    Perman, B.4    Ramyar, K.X.5
  • 37
    • 13244253766 scopus 로고    scopus 로고
    • pdb-care (PDB carbohydrate residue check): a program to support annotation of complex carbohydrate structures in PDB files
    • Lutteke, T., von der Lieth, C.W., pdb-care (PDB carbohydrate residue check): a program to support annotation of complex carbohydrate structures in PDB files. BMC Bioinformatics, 5, 2004, 69.
    • (2004) BMC Bioinformatics , vol.5 , pp. 69
    • Lutteke, T.1    von der Lieth, C.W.2
  • 38
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system
    • Macdonald, J.L., Pike, L.J., Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system. Proc. Natl. Acad. Sci. USA 105 (2008), 112–117.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 112-117
    • Macdonald, J.L.1    Pike, L.J.2
  • 41
    • 0023442604 scopus 로고
    • Fitting curves to data using nonlinear regression: a practical and nonmathematical review
    • Motulsky, H.J., Ransnas, L.A., Fitting curves to data using nonlinear regression: a practical and nonmathematical review. FASEB J. 1 (1987), 365–374.
    • (1987) FASEB J. , vol.1 , pp. 365-374
    • Motulsky, H.J.1    Ransnas, L.A.2
  • 44
    • 85014179927 scopus 로고    scopus 로고
    • The RING 2.0 web server for high quality residue interaction networks
    • Piovesan, D., Minervini, G., Tosatto, S.C., The RING 2.0 web server for high quality residue interaction networks. Nucleic Acids Res. 44 (2016), W367–W374.
    • (2016) Nucleic Acids Res. , vol.44 , pp. W367-W374
    • Piovesan, D.1    Minervini, G.2    Tosatto, S.C.3
  • 45
    • 84988433855 scopus 로고    scopus 로고
    • Regulation of antibody effector functions through IgG Fc N-glycosylation
    • Quast, I., Peschke, B., Lunemann, J.D., Regulation of antibody effector functions through IgG Fc N-glycosylation. Cell Mol. Life Sci. 74 (2017), 837–847.
    • (2017) Cell Mol. Life Sci. , vol.74 , pp. 837-847
    • Quast, I.1    Peschke, B.2    Lunemann, J.D.3
  • 48
    • 84926348347 scopus 로고    scopus 로고
    • Alternative molecular formats and therapeutic applications for bispecific antibodies
    • Spiess, C., Zhai, Q., Carter, P.J., Alternative molecular formats and therapeutic applications for bispecific antibodies. Mol. Immunol. 67 (2015), 95–106.
    • (2015) Mol. Immunol. , vol.67 , pp. 95-106
    • Spiess, C.1    Zhai, Q.2    Carter, P.J.3
  • 49
    • 84879088841 scopus 로고    scopus 로고
    • IgG2 Fc structure and the dynamic features of the IgG CH2-CH3 interface
    • Teplyakov, A., Zhao, Y., Malia, T.J., Obmolova, G., Gilliland, G.L., IgG2 Fc structure and the dynamic features of the IgG CH2-CH3 interface. Mol. Immunol. 56 (2013), 131–139.
    • (2013) Mol. Immunol. , vol.56 , pp. 131-139
    • Teplyakov, A.1    Zhao, Y.2    Malia, T.J.3    Obmolova, G.4    Gilliland, G.L.5
  • 50
    • 84857263421 scopus 로고    scopus 로고
    • Directed evolution of stabilized IgG1-Fc scaffolds by application of strong heat shock to libraries displayed on yeast
    • Traxlmayr, M.W., Faissner, M., Stadlmayr, G., Hasenhindl, C., Antes, B., Ruker, F., Obinger, C., Directed evolution of stabilized IgG1-Fc scaffolds by application of strong heat shock to libraries displayed on yeast. Biochim. Biophys. Acta 1824 (2012), 542–549.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 542-549
    • Traxlmayr, M.W.1    Faissner, M.2    Stadlmayr, G.3    Hasenhindl, C.4    Antes, B.5    Ruker, F.6    Obinger, C.7
  • 51
    • 84867069553 scopus 로고    scopus 로고
    • Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing
    • Traxlmayr, M.W., Hasenhindl, C., Hackl, M., Stadlmayr, G., Rybka, J.D., Borth, N., Grillari, J., Ruker, F., Obinger, C., Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing. J. Mol. Biol. 423 (2012), 397–412.
    • (2012) J. Mol. Biol. , vol.423 , pp. 397-412
    • Traxlmayr, M.W.1    Hasenhindl, C.2    Hackl, M.3    Stadlmayr, G.4    Rybka, J.D.5    Borth, N.6    Grillari, J.7    Ruker, F.8    Obinger, C.9
  • 54
    • 77954638589 scopus 로고    scopus 로고
    • Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties
    • Wozniak-Knopp, G., Bartl, S., Bauer, A., Mostageer, M., Woisetschläger, M., Antes, B., Ettl, K., Kainer, M., Weberhofer, G., Wiederkum, S., et al. Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties. Protein Eng. Des. Sel. 23 (2010), 289–297.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 289-297
    • Wozniak-Knopp, G.1    Bartl, S.2    Bauer, A.3    Mostageer, M.4    Woisetschläger, M.5    Antes, B.6    Ettl, K.7    Kainer, M.8    Weberhofer, G.9    Wiederkum, S.10
  • 55
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright, P.E., Dyson, H.J., Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999), 321–331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 56
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang, Y., Skolnick, J., Scoring function for automated assessment of protein structure template quality. Proteins 57 (2004), 702–710.
    • (2004) Proteins , vol.57 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.