메뉴 건너뛰기




Volumn 289, Issue 10, 2014, Pages 7200-7210

Conformational heterogeneity in antibody-protein antigen recognition: Implications for high affinity protein complex formation

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; ANTIGENS;

EID: 84896758400     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.492215     Document Type: Article
Times cited : (12)

References (38)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G., and Milstein, C. (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 2
    • 78649708348 scopus 로고    scopus 로고
    • Current perspectives on therapeutic antibodies
    • Yoon, S., Kim, Y. S., Shim, H., and Chung, J. (2010) Current perspectives on therapeutic antibodies. Biotech. Bioproc. Eng. 15, 709-715
    • (2010) Biotech. Bioproc. Eng. , vol.15 , pp. 709-715
    • Yoon, S.1    Kim, Y.S.2    Shim, H.3    Chung, J.4
  • 3
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger, P., and Hudson, P. J. (2005) Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 23, 1126-1136
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 4
    • 78649669018 scopus 로고    scopus 로고
    • Metrics for antibody therapeutics development
    • Reichert, J. M. (2010) Metrics for antibody therapeutics development. MAbs 2, 695-700
    • (2010) MAbs , vol.2 , pp. 695-700
    • Reichert, J.M.1
  • 5
    • 84868584302 scopus 로고    scopus 로고
    • A systematic comparison of free and bound antibodies reveals binding-related conformational changes
    • Sela-Culang, I., Alon, S., and Ofran, Y. (2012) A systematic comparison of free and bound antibodies reveals binding-related conformational changes. J. Immunol. 189, 4890-4899
    • (2012) J. Immunol. , vol.189 , pp. 4890-4899
    • Sela-Culang, I.1    Alon, S.2    Ofran, Y.3
  • 6
    • 38349018735 scopus 로고    scopus 로고
    • Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints
    • Grishaev, A., Tugarinov, V., Kay, L. E., Trewhella, J., and Bax, A. (2008) Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. J. Biomol. NMR 40, 95-106
    • (2008) J. Biomol. NMR , vol.40 , pp. 95-106
    • Grishaev, A.1    Tugarinov, V.2    Kay, L.E.3    Trewhella, J.4    Bax, A.5
  • 8
    • 34547410355 scopus 로고    scopus 로고
    • Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A
    • Waters, L. C., Veverka, V., Böhm, M., Schmedt, T., Choong, P. T., Muskett, F. W., Klempnauer, K. H., and Carr, M. D. (2007) Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A. Oncogene 26, 4941-4950
    • (2007) Oncogene , vol.26 , pp. 4941-4950
    • Waters, L.C.1    Veverka, V.2    Böhm, M.3    Schmedt, T.4    Choong, P.T.5    Muskett, F.W.6    Klempnauer, K.H.7    Carr, M.D.8
  • 9
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • Williamson, R. A., Carr, M. D., Frenkiel, T. A., Feeney, J., and Freedman, R. B. (1997) Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry 36, 13882-13889
    • (1997) Biochemistry , vol.36 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 10
    • 0034636978 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 undergoes microsecond to millisecond motions at sites of matrix metalloproteinase-induced fit
    • Gao, G., Semenchenko, V., Arumugam, S., and Van Doren, S. R. (2000) Tissue inhibitor of metalloproteinases-1 undergoes microsecond to millisecond motions at sites of matrix metalloproteinase-induced fit. J. Mol. Biol. 301, 537-552
    • (2000) J. Mol. Biol. , vol.301 , pp. 537-552
    • Gao, G.1    Semenchenko, V.2    Arumugam, S.3    Van Doren, S.R.4
  • 12
    • 0033601381 scopus 로고    scopus 로고
    • The effect of matrix metalloproteinase complex formation on the conformational mobility of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Williamson, R. A., Muskett, F. W., Howard, M. J., Freedman, R. B., and Carr, M. D. (1999) The effect of matrix metalloproteinase complex formation on the conformational mobility of tissue inhibitor of metalloproteinases-2 (TIMP-2). J. Biol. Chem. 274, 37226-37232
    • (1999) J. Biol. Chem. , vol.274 , pp. 37226-37232
    • Williamson, R.A.1    Muskett, F.W.2    Howard, M.J.3    Freedman, R.B.4    Carr, M.D.5
  • 13
    • 0035980017 scopus 로고    scopus 로고
    • Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14
    • Williamson, R. A., Hutton, M., Vogt, G., Rapti, M., Knäuper, V., Carr, M. D., and Murphy, G. (2001) Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14. J. Biol. Chem. 276, 32966-32970
    • (2001) J. Biol. Chem. , vol.276 , pp. 32966-32970
    • Williamson, R.A.1    Hutton, M.2    Vogt, G.3    Rapti, M.4    Knäuper, V.5    Carr, M.D.6    Murphy, G.7
  • 14
    • 70450274968 scopus 로고    scopus 로고
    • High resolution NMR-based model for the structure of a scFv-IL-1 complex: Potential for NMR as a key tool in therapeutic antibody design and development
    • Wilkinson, I. C., Hall, C. J., Veverka, V., Shi, J. Y., Muskett, F. W., Stephens, P. E., Taylor, R. J., Henry, A. J., and Carr, M. D. (2009) High resolution NMR-based model for the structure of a scFv-IL-1 complex: potential for NMR as a key tool in therapeutic antibody design and development. J. Biol. Chem. 284, 31928-31935
    • (2009) J. Biol. Chem. , vol.284 , pp. 31928-31935
    • Wilkinson, I.C.1    Hall, C.J.2    Veverka, V.3    Shi, J.Y.4    Muskett, F.W.5    Stephens, P.E.6    Taylor, R.J.7    Henry, A.J.8    Carr, M.D.9
  • 15
    • 84873961029 scopus 로고    scopus 로고
    • Conservation of functional sites on interleukin-6 and implications for evolution of signaling complex assembly and therapeutic intervention
    • Veverka, V., Baker, T., Redpath, N. T., Carrington, B., Muskett, F. W., Taylor, R. J., Lawson, A. D., Henry, A. J., and Carr, M. D. (2012) Conservation of functional sites on interleukin-6 and implications for evolution of signaling complex assembly and therapeutic intervention. J. Biol. Chem. 287, 40043-40050
    • (2012) J. Biol. Chem. , vol.287 , pp. 40043-40050
    • Veverka, V.1    Baker, T.2    Redpath, N.T.3    Carrington, B.4    Muskett, F.W.5    Taylor, R.J.6    Lawson, A.D.7    Henry, A.J.8    Carr, M.D.9
  • 16
    • 0001615271 scopus 로고
    • Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen, J. (1958) Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. U.S.A. 44, 1072-1078
    • (1958) Proc. Natl. Acad. Sci. U.S.A. , vol.44 , pp. 1072-1078
    • Spizizen, J.1
  • 17
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C., and Spizizen, J. (1961) Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81, 741-746
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 18
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • Sivashanmugam, A., Murray, V., Cui, C., Zhang, Y., Wang, J., and Li, Q. (2009) Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci. 18, 936-948
    • (2009) Protein Sci. , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5    Li, Q.6
  • 19
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 20
    • 84859396347 scopus 로고    scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. 1990
    • Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (2011) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. 1990. J. Magn. Reson. 213, 423-441
    • (2011) J. Magn. Reson. , vol.213 , pp. 423-441
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 21
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3DNMR experiment to correlate amide-proton and nitrogen resonances with the and carbon resonances in proteins
    • Wittekind, M., and Mueller, L. (1993) HNCACB, a high-sensitivity 3DNMR experiment to correlate amide-proton and nitrogen resonances with the and carbon resonances in proteins. J. Magn. Reson. B 101, 201-205
    • (1993) J. Magn. Reson. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 22
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S., and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 23
    • 0342326257 scopus 로고    scopus 로고
    • Gradient and sensitivity enhancement of 2D TROSY with water flip-back, 3D NOESY-TROSY and TOCSY-TROSY experiments
    • Zhu, G., Kong, X. M., and Sze, K. H. (1999) Gradient and sensitivity enhancement of 2D TROSY with water flip-back, 3D NOESY-TROSY and TOCSY-TROSY experiments. J. Biomol. NMR 13, 77-81
    • (1999) J. Biomol. NMR , vol.13 , pp. 77-81
    • Zhu, G.1    Kong, X.M.2    Sze, K.H.3
  • 24
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • Kontaxis, G., Clore, G. M., and Bax, A. (2000) Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143, 184-196
    • (2000) J. Magn. Reson. , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 25
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A proteinprotein docking approach based on biochemical or biophysical data
    • Dominguez, C., Boelens, R., and Bonvin, A. (2003) HADDOCK: a proteinprotein docking approach based on biochemical or biophysical data. J. Am. Chem. Soc. 125, 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.3
  • 26
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of 1H, 13C, and 15N spectra of larger proteins: Heteronuclear triple resonance three-dimensional NMR spectroscopy
    • Ikura, M., Kay, L. E., and Bax, A. (1990) A novel approach for sequential assignment of 1H, 13C, and 15N spectra of larger proteins: heteronuclear triple resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29, 4659-4667
    • (1990) Application to Calmodulin. Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 27
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax, A. (1994) Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol. 4, 738-744
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 738-744
    • Bax, A.1
  • 28
    • 38449103508 scopus 로고    scopus 로고
    • NMR methods for studying protein-protein interactions involved in translation initiation
    • Marintchev, A., Frueh, D., and Wagner, G. (2007) NMR methods for studying protein-protein interactions involved in translation initiation. Methods Enzymol. 430, 283-331
    • (2007) Methods Enzymol. , vol.430 , pp. 283-331
    • Marintchev, A.1    Frueh, D.2    Wagner, G.3
  • 29
    • 0030239095 scopus 로고    scopus 로고
    • Complete 1H, 15Nand 13Cassignments, secondary structure, and topology of recombinant human interleukin-6
    • Xu, G. Y., Hong, J., McDonagh, T., Stahl, M., Kay, L. E., Seehra, J., and Cumming, D. A. (1996) Complete 1H, 15Nand 13Cassignments, secondary structure, and topology of recombinant human interleukin-6. J. Biomol. NMR 8, 123-135
    • (1996) J. Biomol. NMR , vol.8 , pp. 123-135
    • Xu, G.Y.1    Hong, J.2    McDonagh, T.3    Stahl, M.4    Kay, L.E.5    Seehra, J.6    Cumming, D.A.7
  • 30
    • 0025210153 scopus 로고
    • Complete resonance assignment for the polypeptide backbone of interleukin-1 using three-dimensional heteronuclear NMR spectroscopy
    • Driscoll, P. C., Clore, G. M., Marion, D., Wingfield, P. T., and Gronenborn, A. M (1990) Complete resonance assignment for the polypeptide backbone of interleukin-1 using three-dimensional heteronuclear NMR spectroscopy. Biochemistry 29, 3542-3556
    • (1990) Biochemistry , vol.29 , pp. 3542-3556
    • Driscoll, P.C.1    Clore, G.M.2    Marion, D.3    Wingfield, P.T.4    Gronenborn, A.M.5
  • 31
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 receptor/ gp130 complex
    • Boulanger, M. J., Chow, D. C, Brevnova, E. E., and Garcia, K. C. (2003) Hexameric structure and assembly of the interleukin-6/IL-6 receptor/ gp130 complex. Science 300, 2101-2104
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 33
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 34
    • 0025151612 scopus 로고
    • Small rearrangements in structures of Fv and Fab fragments of antibody D 1. 3 on antigen binding
    • Bhat, T. N., Bentley, G. A., Fischmann, T. O., Boulot, G., and Poljak, R. J. (1990) Small rearrangements in structures of Fv and Fab fragments of antibody D 1.3 on antigen binding. Nature 347, 483-485
    • (1990) Nature , vol.347 , pp. 483-485
    • Bhat, T.N.1    Bentley, G.A.2    Fischmann, T.O.3    Boulot, G.4    Poljak, R.J.5
  • 35
    • 0023090513 scopus 로고
    • Three-dimensional structure of a complex of antibody with influenza virus neuraminidase
    • Colman, P. M., Laver, W. G., Varghese, J. N., Baker, A. T., Tulloch, P. A., Air, G. M., and Webster, R. G. (1987) Three-dimensional structure of a complex of antibody with influenza virus neuraminidase. Nature 326, 358-363
    • (1987) Nature , vol.326 , pp. 358-363
    • Colman, P.M.1    Laver, W.G.2    Varghese, J.N.3    Baker, A.T.4    Tulloch, P.A.5    Air, G.M.6    Webster, R.G.7
  • 36
    • 0000441957 scopus 로고
    • Twisting into shape
    • Davies, D. R., and Padlan, E. A. (1992) Twisting into shape. Curr. Biol. 2, 254-256
    • (1992) Curr. Biol. , vol.2 , pp. 254-256
    • Davies, D.R.1    Padlan, E.A.2
  • 38
    • 84870938343 scopus 로고    scopus 로고
    • Proteasome allostery as a population shift between interchanging conformers
    • Ruschak, A. M., and Kay, L. E. (2012) Proteasome allostery as a population shift between interchanging conformers. Proc. Natl. Acad. Sci. U.S.A. 109, E3454-3462
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Ruschak, A.M.1    Kay, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.