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Volumn 259, Issue 5, 1996, Pages 938-946

X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form

Author keywords

Antibody structure; Antibody antigen interaction; Induced fit; Mobility; Structure comparison

Indexed keywords

CANCER ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT;

EID: 0030604686     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0371     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 0027299695 scopus 로고
    • Three-dimensional structure of an anti-steroid Fab' and progesterone-Fab' complex
    • Arevalo, J. H., Stura, E. A., Taussig, M. J. & Wilson, I. A. (1993a). Three-dimensional structure of an anti-steroid Fab' and progesterone-Fab' complex. J. Mol. Biol. 231, 103-118.
    • (1993) J. Mol. Biol. , vol.231 , pp. 103-118
    • Arevalo, J.H.1    Stura, E.A.2    Taussig, M.J.3    Wilson, I.A.4
  • 2
    • 0027686741 scopus 로고
    • Molecular basis of crossreactivity and the limits of antibody-antigen complementarity
    • Arevalo, J. H., Taussig, M. J. & Wilson, I. A. (1993b). Molecular basis of crossreactivity and the limits of antibody-antigen complementarity. Nature, 365, 859-863.
    • (1993) Nature , vol.365 , pp. 859-863
    • Arevalo, J.H.1    Taussig, M.J.2    Wilson, I.A.3
  • 5
    • 0028014681 scopus 로고
    • Crystallization and preliminary X-ray analysis of the monoclonal anti-tumor antibody BR96 and its complex with the Lewis Y determinant
    • Chang, C. Y., Jeffrey, P. D., Bajorath, J., Hellström, I., Hellström, K. E. & Sheriff, S. (1994). Crystallization and preliminary X-ray analysis of the monoclonal anti-tumor antibody BR96 and its complex with the Lewis Y determinant. J. Mol. Biol. 235, 372-376.
    • (1994) J. Mol. Biol. , vol.235 , pp. 372-376
    • Chang, C.Y.1    Jeffrey, P.D.2    Bajorath, J.3    Hellström, I.4    Hellström, K.E.5    Sheriff, S.6
  • 7
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M. L. (1983). Analytical molecular surface calculation. J. Appl. Crystallog. 16, 548-558.
    • (1983) J. Appl. Crystallog. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 8
    • 0000144850 scopus 로고
    • (Rossmann, M. G., ed.), Gordon and Breach, New York
    • Crowther, R. A. (1972). In The Molecular Replacement Method (Rossmann, M. G., ed.), pp. 173-178, Gordon and Breach, New York.
    • (1972) The Molecular Replacement Method , pp. 173-178
    • Crowther, R.A.1
  • 9
    • 84944816398 scopus 로고
    • Application of the molecular replacement method to multidomain proteins. 1. Determination of the orientation of an immunoglobulin Fab fragment
    • Cygler, M. & Anderson, W. F. (1988). Application of the molecular replacement method to multidomain proteins. 1. Determination of the orientation of an immunoglobulin Fab fragment. Acta Crystallog. sect. A, 44, 38-55.
    • (1988) Acta Crystallog. Sect. A , vol.44 , pp. 38-55
    • Cygler, M.1    Anderson, W.F.2
  • 10
    • 0026319774 scopus 로고
    • Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment
    • Cygler, M., Rose, D. R. & Bundle, D. R. (1991). Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science, 253, 442-445.
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 11
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , Issue.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 84967852329 scopus 로고
    • MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald, P. M. D. (1988). MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Crystallog. 21, 273-278.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 14
    • 85055704314 scopus 로고
    • Experiences with a new translation-function program. J
    • Fujinaga, M. & Read, R. J. (1987). Experiences with a new translation-function program. J. Appl. Crystallog. 20, 517-521.
    • (1987) Appl. Crystallog. , vol.20 , pp. 517-521
    • Fujinaga, M.1    Read, R.J.2
  • 16
    • 0028273713 scopus 로고
    • Anti-tumor antibody BR96 blocks cell migration and binds to lysosomal membrane glycoprotein on cell surface microspikes and ruffled membranes
    • Garrigues, J., Anderson, J., Hellström, K. E. & Hellström, I. (1994). Anti-tumor antibody BR96 blocks cell migration and binds to lysosomal membrane glycoprotein on cell surface microspikes and ruffled membranes. J. Cell. Biol. 125, 129-142.
    • (1994) J. Cell. Biol. , vol.125 , pp. 129-142
    • Garrigues, J.1    Anderson, J.2    Hellström, K.E.3    Hellström, I.4
  • 17
    • 0018780591 scopus 로고
    • Side-chain torsional potentials: Effect of dipeptide, protein and solvent environment
    • Gelin, B. R. & Karplus, M. (1979). Side-chain torsional potentials: effect of dipeptide, protein and solvent environment. Biochemistry, 18, 1256-1268.
    • (1979) Biochemistry , vol.18 , pp. 1256-1268
    • Gelin, B.R.1    Karplus, M.2
  • 18
    • 0026679890 scopus 로고
    • The three-dimensional structure of an intact monoclonal antibody for canine lymphoma
    • Harris, L. J., Larson, S. B., Hasel, K. W., Day, J., Greenwood, A. & McPherson, A. (1992). The three-dimensional structure of an intact monoclonal antibody for canine lymphoma. Nature, 360, 369-372.
    • (1992) Nature , vol.360 , pp. 369-372
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    Day, J.4    Greenwood, A.5    McPherson, A.6
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5, 802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 26
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution
    • Marquart, M., Deisenhofer, J., Huber, R. & Palm, W. (1980). Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution. J. Mol. Biol. 141, 369-391.
    • (1980) J. Mol. Biol. , vol.141 , pp. 369-391
    • Marquart, M.1    Deisenhofer, J.2    Huber, R.3    Palm, W.4
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 28
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34, 167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 29
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini, J. M., Schulze-Gahmen, U. & Wilson, I. A. (1992). Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science, 255, 959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 30
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack, J. S. (1988). CHAIN - a crystallographic modeling program. J. Mol. Graph. 6, 224-225.
    • (1988) J. Mol. Graph. , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 31
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 Å
    • Satow, Y., Cohen, G. H., Padlan, E. A. & Davies, D. R. (1986). Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 Å. J. Mol. Biol. 190, 593-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 32
    • 0027133936 scopus 로고
    • Detailed analysis of the free and bound conformations of an antibody: X-ray structures of Fab 17/9 and three different Fab-peptide complexes
    • Schulze-Gahmen, U., Rini, J. M. & Wilson, I. A. (1993). Detailed analysis of the free and bound conformations of an antibody: X-ray structures of Fab 17/9 and three different Fab-peptide complexes. J. Mol. Biol. 234, 1098-1118.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1098-1118
    • Schulze-Gahmen, U.1    Rini, J.M.2    Wilson, I.A.3
  • 33
    • 0000541786 scopus 로고
    • Some methods for examining the interactions between two molecules
    • Sheriff, S. (1993). Some methods for examining the interactions between two molecules. ImmunoMethods, 3, 191-196.
    • (1993) Immunomethods , vol.3 , pp. 191-196
    • Sheriff, S.1
  • 34
    • 0347912957 scopus 로고
    • Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins
    • Sheriff, S., Hendrickson, W. A., Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. (1985). Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins. Proc. Natl Acad. Sci. USA, 82, 1104-1107.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1104-1107
    • Sheriff, S.1    Hendrickson, W.A.2    Stenkamp, R.E.3    Sieker, L.C.4    Jensen, L.H.5
  • 35
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • Sheriff, S., Hendrickson, W. A. & Smith, J. L. (1987). Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197, 273-296.
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 36
    • 0026575750 scopus 로고
    • Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering
    • Sosnick, T. R., Benjamin, D. C., Novotny, J., Seeger, P. A. & Trewhella, J. (1992). Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering. Biochemistry, 31, 1779-1786.
    • (1992) Biochemistry , vol.31 , pp. 1779-1786
    • Sosnick, T.R.1    Benjamin, D.C.2    Novotny, J.3    Seeger, P.A.4    Trewhella, J.5
  • 37
    • 0025321903 scopus 로고
    • Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å
    • Stanfield, R. L., Fieser, T. M., Lerner, R. A. & Wilson, I. A. (1990). Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å. Science, 248, 712-719.
    • (1990) Science , vol.248 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 39
    • 0026631064 scopus 로고
    • Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
    • Steipe, B., Plückthun, A. & Huber, R. (1992). Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant. J. Mol. Biol. 225, 739-753.
    • (1992) J. Mol. Biol. , vol.225 , pp. 739-753
    • Steipe, B.1    Plückthun, A.2    Huber, R.3
  • 40
    • 0028304866 scopus 로고
    • Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2
    • Tormo, J., Blaas, D., Parry, N. R., Rowlands, D., Stuart, D. & Fita, I. (1994). Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. EMBO J. 13, 2247-2256.
    • (1994) EMBO J , vol.13 , pp. 2247-2256
    • Tormo, J.1    Blaas, D.2    Parry, N.R.3    Rowlands, D.4    Stuart, D.5    Fita, I.6
  • 44
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I. A. & Stanfield, R. L. (1994). Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.