Comparative Structures of Mouse Antibody Combining Sites

  • David R. Davies
  • Talapady N. Bhat
  • Gerson H. Cohen
  • Eduardo A. Padlan
Part of the Methodological Surveys in Biochemistry and Analysis book series (MSBA, volume 15B)


The crystal structures of two mouse myeloma antibody-binding fragments (Fab’s) have been determined: McPC603, an anti-phosphocholine immunoglobulin (anti-PC Ig), and J539 which is specific for galactan. A comparison has been made between the sequences of other mouse Ig’s that have similar binding properties. In both heavy and light chains of the PC-binding proteins, the residues in contact with the PC remain invariant or highly conserved. Examination of the pattern of charge conservation at the combining site reveals a possible coupling of somatic mutations in order to maintain specificity.


Light Chain Heavy Chain Central Cavity Chain Sequence Amino Acid Sequence Information 
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  1. 1.
    Köhler, G. & Milstein, C. (1975) Nature 256, 495–497.CrossRefGoogle Scholar
  2. 2.
    Silverton, E.W., Davies, D.R., Smith-Gill, S. & Potter, M. (1983) Abs. Am. Crystallographic Assn. 11 (2), 28.Google Scholar
  3. 3.
    Mariuzza, R.A., Jankovic, D.L., Boulot, G., Amit, A.G., Saludjian, P., LeGuern, A., Mazie, J.C. & Poljak, R.J. (1983) J. Mot. Biol. 170, 1055–1058.CrossRefGoogle Scholar
  4. 4.
    Bernstein, F.C., Koetzke, T.F., Williams, G.J.B., Meyer, E.F., Brice, M.D., Rogers, J.R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977) J. Mol. Biol. 112, 535–542.CrossRefGoogle Scholar
  5. 5.
    Padlan, E.A., Segal, D.M., Rudikoff, S., Potter, M., Spande, T.F. & Davies, D.R. (1973) Nature New Biol. 245, 165–167.Google Scholar
  6. 6.
    Segal, D.M., Padlan, E.A., Cohen, G.H., Rudikoff, S., Potter, M. & Davies, D.R. (1974) Proc. Nat. Acad. Sci. 71, 4298–4302.CrossRefGoogle Scholar
  7. 7.
    Padlan, E.A., Davies, D.R., Rudikoff, S. & Potter, M. (1976) Immunochemistry 13, 945–949.CrossRefGoogle Scholar
  8. 8.
    Davies, D.R. & Metzger, H. (1983) Ann. Rev.Immunol.1,87–117.Google Scholar
  9. 9.
    Kabat, E.A., Wu, T.T., Bilofsky, H., Reid-Miller, M. & Perry, H. (1983) Sequences of Proteins of Immunological Interest, National Institutes of Health, Bethesda, MD. [Cf. E.A. Kabat, this vol.-Ed.]Google Scholar
  10. 10.
    Gearhart, P., Johnson, N.D., Douglas, R. & Hood, L. (1981) Nature 291, 29–34.CrossRefGoogle Scholar
  11. 11.
    Rudikoff, S. (1983) in Contemporary Topics in Molecular Immunology, Vol. 9 (Inman, F.P. & Kindt, T.J., eds.), Plenum, New York, pp. 169–209.Google Scholar
  12. 12.
    Navia, M.A., Segal, D.M., Padlan, E.A., Davies, D.R., Rao, D.N., Rudikoff, S. & Potter, M. (1979) Proc. Nat. Acad. Sci. 76, 4071–4074.CrossRefGoogle Scholar
  13. 13.
    Saul, F., Amzel, L.M. & Poljak, R.J. (1978) J. Biol. Chem. 253, 585–597.Google Scholar
  14. 14.
    Silverton, E.W., Navia, M.A. & Davies, D.R. (1977) Proc. Nat. Acad. Sci. 74, 5140 - -5144.Google Scholar
  15. 15.
    Marquart, M., Deisenhofer, J., Huber, R. & Palm, W. (1980) J. Mol. Biol. 141, 369–391.CrossRefGoogle Scholar
  16. 16.
    Manjula, B.N. & Glaudemans, C.P.J. (1976) Immunochemistry 13, 469–471.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • David R. Davies
    • 1
  • Talapady N. Bhat
    • 1
  • Gerson H. Cohen
    • 1
  • Eduardo A. Padlan
    • 1
  1. 1.Laboratory of Molecular BiologyNational Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases National Institutes of HealthBethesdaUSA

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