SEARCH

SEARCH BY CITATION

References

  • 1
    Amit, A.G., Mariuzza, R.A., Phillips, S.E.V, & Poljak, R.J. (1985). Three-dimensional structure of an antigen-antibody complex at 6 Å resolution. Nature 313, 156158.
  • 2
    Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F., Jr., Brice, M.D., Rodgers, J.D., Kennard, O., Shimanouchi, T., & Tasoumi, M. (1977). The Protein Data Bank: A computer archival file for macromolecular structures. J. Mol. Biol. 112, 535542.
  • 3
    Bhat, T.N., Bentley, G.A., Fischmann, T.O., Boulot, G., & Poljak, R.J. (1990). Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature 347, 483485.
  • 4
    Brunger, A.T. (1988). Crystallographic refinement by simulated annealing. J. Mol. Biol. 203, 803816.
  • 5
    Bundle, D.R. (1989). Antibody combining sites and oligosaccharide determinants studied by competitive binding, sequencing and X-ray crystallography. Pure Appl. Chem. 61, 11711180.
  • 6
    Bundle, D.R., Cherwonogrodzky, J.W., Gidney, M.A.J., Meikle, P.J., Perry, M.B., & Peters, T. (1989). Definition of Brucella A and M epitopes by monoclonal typing reagents and synthetic oligosaccharides. Infect. Immun. 57, 28292836.
  • 7
    Bundle, D.R., Gidney, M.A.J., Perry, M.B., Duncan, J.R., & Cherwonogrodzky, J.W. (1984). Serological confirmation of Brucella abortus and Yersinia enterocolitica O:9 O-antigens by monoclonal antibodies. Infect. Immun. 46, 389393.
  • 8
    Chothia, C. & Lesk, A. (1987). Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 901917.
  • 9
    Chothia, C., Lesk, A.M., Tramontano, A., Levitt, M., Smith-Gill, S.J., Air, G., Sheriff, S., Padlan, E.A., Davies, D., Tulip, W.R., Colman, P.M., Spinelli, S., Alzari, P.M., & Poljak, R.J. (1989). Conformations of immunoglobulin hypervariable regions. Nature 242, 877883.
  • 10
    Cisar, J., Kabat, E.A., Dorner, M.N., & Liao, J. (1975). Binding properties of immunoglobulin combining sites specific for terminal or nonterminal antigenic determinants in dextran. J. Exp. Med. 142, 435459.
  • 11
    Colman, P.M., Tulloch, P.A., Gough, J.H., Varghese, J.N., Laver, W.G., & Webster, R.C. (1985). The structure of an antineuraminidase monoclonal Fab fragment and its interaction with the antigen. In Immune Recognition of Protein Antigens (Laver, W.G. & Air, G.M., Eds.), pp. 7790. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
  • 12
    Crews, S., Griffin, J., Huang, H., Calame, K., & Hood, L. (1981). A single VH gene segment encodes the immune response to phosphocholine: Somatic mutation is correlated with the class of the antibody. Cell 25, 5968.
  • 13
    Crowther, R.A. (1972). The fast rotation function. In The Molecular Replacement Method (Rossmann, M.G., Ed.), pp. 173178. Gordon & Breach, New York.
  • 14
    Cygler, M., Boodhoo, A., Lee, J.S., & Anderson, W.F. (1987). Crystallization and structure determination of an autoimmune antipoly(dT) immunoglobulin Fab fragment at 3.0 Å resolution. J. Biol. Chem. 262, 643648.
  • 15
    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, 442445.
  • 16
    Evans, S.V. (1993). SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics, in press.
  • 17
    Fujinaga, M. & Read, R. (1987). Experiences with a new translation function program. J. Appl. Crystallogr. 20, 517521.
  • 18
    Hakomori, S. (1984). Tumour-associated carbohydrate antigens. Annu. Rev. Immunol. 2, 103126.
  • 19
    Hendrickson, W.A. & Konnert, J.H. (1979). Stereochemically restrained crystallographic least-squares refinement of macromolecule structures. In Biomolecular Structure, Conformation, Function & Evolution, Vol. 1 (Srinivasan, R., Ed.), pp. 4357. Pergamon Press, New York.
  • 20
    Jones, T.A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268272.
  • 21
    Lascombe, M.-B., Alzari, P.M., Boulot, G., Saludjian, P., Tougard, P., Berek, C., Haba, S., Rosen, E.M., Nisonoff, A., & Poljak, R.J. (1989). Three-dimensional structure of Fab R19.9, a monoclonal murine antibody specific for the p-azobenzenearsonate group. Proc. Natl. Acad. Sci. USA 86, 607611.
  • 22
    Lindberg, A.A., Wollin, R., Bruse, G., Ekwall, E., & Svenson, S. (1983). Immunology and immunochemistry of synthetic and semi-synthetic Salmonella O-antigen-specific glycoconjugates. Am. Chem. Soc. Symp. Ser. 231, 83118.
  • 23
    Matsushima, M., Marquart, M., Jones, T.A., Colman, P.M., Bartels, K., Huber, R., & Palm, W. (1978). Crystal structure of the human Fab fragment KOL and its comparison with the intact KOL molecule. J. Mol. Biol. 121, 441459.
  • 24
    Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491497.
  • 25
    Meek, K., Sanz, I., Rathbun, G., Nisonoff, A., & Capra, J.D. (1987). Identity of the Vk10-Ars-A gene segments of the A/J and BALB/c strains. Proc. Natl. Acad. Sci. USA 84, 62446248.
  • 26
    Meikle, P.J., Perry, M.B., Cherwonogrodzky, J.W., & Bundle, D.R. (1989). The fine structure of A and M antigens from Brucella biovars. Infect. Immun. 57, 28202828.
  • 27
    Morris, A.L., MacArthur, M.W., Hutchinson, E.G., & Thornton, J.M. (1992). Stereochemical quality of protein structure coordinates. Proteins Struct. Funct. Genet. 12, 345364.
  • 28
    Novotny, J. & Haber, E. (1985). Structural invariants of antigen binding: Comparison of immunoglobulin VL-VH and VL-VL domain dimers. Proc. Natl. Acad. Sci. USA 82, 45924596.
  • 29
    Oomen, R., Young, N.M., & Bundle, D.R. (1991). Molecular modelling of antibody-antigen complexes between the Brucella abortus O-chain polysaccharide and a specific monoclonal antibody. Protein Eng. 4, 427431.
  • 30
    Peters, T., Brisson, J.-R., & Bundle, D.R. (1990). Conformational analysis of key disaccharide components of Brucella A and M antigens. Can. J. Chem. 68, 979988.
  • 31
    Przybylska, M. (1989). A double cell for controlling nucleation and growth of protein crystals. J. Appl. Crystallogr. 22, 115118.
  • 32
    Quiocho, F.A. (1989). Protein-carbohydrate interactions–Basic molecular features. Pure Appl. Chem. 61, 12931306.
  • 33
    Read, R. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140149.
  • 34
    Rini, J.M., Schulze-Gahman, U., & Wilson, I.A. (1992). Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255, 959965.
  • 35
    Satow, Y., Cohen, G.H., Padlan, E.A., & Davies, D.R. (1987). Phosphocholine binding immunoglobulin Fab MC/PC603. An X-ray diffraction study at 2.7 Å. J. Mol. Biol. 190, 593604.
  • 36
    Sheriff, S., Silverton, E.W., Padlan, E.A., Cohen, G.H., Smith-Gill, S.J., Finzel, S.C., & Davies, D.R. (1987). The three-dimensional structure of an antibody-antigen complex. Proc. Natl. Acad. Sci. USA 84, 80758079.
  • 37
    Strong, R.K., Campbell, R.L., Rose, D.R., Petsko, G.A., Sharon, J., & Margolies, M.N. (1991). The three-dimensional structure of the murine anti-phenylarsonate Fab 36–71 I: X-ray crystallography and modelling of the complex with hapten. Biochemistry 30, 37393748.
  • 38
    Suh, S.W., Bhat, T.N., Naira, M.A., Cohen, G.H., Rao, D.N., Rudikoff, S., & Davies, D.R. (1986). The galactan-binding immunoglobulin Fab J539: An X-ray diffraction study at 2.6 Å resolution. Proteins Struct. Funct. Genet. 1, 7580.
  • 39
    Weininger, M.S. & Banaszak, L.J. (1978). Mitochondrial malate dehydrogenase. Crystallographic properties of the pig heart enzyme. J. Mol. Biol. 119, 443449.