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The structure determination of the variable portion of the Bence-Jones protein Au

Abstract

The structure of a χ-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur. J. Biochem. 45, 513 (1974)). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 å. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones and of the internal residues is extremely similar to that found in Rei.

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References

  1. Crowther, B. A.: The molecular replacement method. A collection of papers on the use of noncrystallographic symmetry (M. G. Rossman, ed.), pp. 173–178. New York, London, Paris: Gordon and Breach, Science publishers 1972

    Google Scholar 

  2. Crowther, R. A., Blow, D. M.: A method of positioning a known molecule in an unknown crystal structure. Acta Cryst. 23, 544–548 (1967)

    Google Scholar 

  3. Deisenhofer, J., Steigemann, W.: In: 2nd International Research Conference on Proteinase Inhibitors (Bayer Symposium V) (H. Fritz, H. Tschesche, L. J. Greene, E. Truscheit, eds.). Berlin-Heidelberg-New York: Springer (in press)

  4. Diamond, R.: A real-space refinement procedure for proteins. Acta Cryst. A 27, 436–452 (1971)

    Google Scholar 

  5. Epp, O., Palm, W., Fehlhammer, H., Rühlmann, A., Steigemann, W., Schwager, P., Huber, R.: Crystallographic evidence for structurally similar domains in the human χ-type Bence-Jones Protein Rei. J. molec. Biol. 69, 315–318 (1972)

    Google Scholar 

  6. Epp, O., Colman, P., Fehlhammer, H., Bode, W., Schiffer, M., Huber, R., Palm, W.: Crystal and molecular structure of a Dimer composed of the variable portion of the Bence-Jones protein Rei. Europ. J. Biochem. 45, 513–524 (1974)

    Google Scholar 

  7. Hoppe, W.: Die Faltmolekülmethode und ihre Anwendung in der röntgenographischen Konstitutionsanalyse von Biflorin (C20H20O4). Elektrochemie 61, 1076–1083 (1957)

    Google Scholar 

  8. Huber, R.: Die automatisierte Faltmolekülmethode. Acta Cryst. 19, 353–356 (1965)

    Google Scholar 

  9. Huber, R.: In: Crystallographic computing (F. R. Ahmed, ed.), pp. 96–102. Copenhagen: Munksgaard 1969

    Google Scholar 

  10. Huber, R., Kopfmann., G.: Experimental absorption correction: Results: Acta Cryst. A 25, 143–152 (1969)

    Google Scholar 

  11. Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., Steigemann, W.: Structure of the complex formed by Bovine trypsin and Bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 å resolution. J. molec. Biol. 88, (1974) (in press)

  12. Palm, W.: The isolation, characterisation and crystallisation of a human Bence-Jones protein of χ-type. FEBS Lett. 10, 46–48 (1970)

    Google Scholar 

  13. Palm, W., Hilschmann, N.: Die PrimÄrstruktur einer kristallinen monoklinalen Immun-globulin-L-Kette vom χ-Typ, Subgruppe I (Bence-Jones Protein Rei): Ein Beitrag zur AufklÄrung der dreidimensionalen Struktur der Immunglobuline. Hoppe-Seylers Z. physiol. Chem. 354, 1651–1654 (1973)

    Google Scholar 

  14. Poljak, R. J., Amzel, L. M., Avey, H. P., Chen, B. L., Phizackerley, R. P., Saul, F.: Three-dimensional structure of the Fab' fragment of the human immunglobulin at 2.8 å resolution. Proc. nat. Acad. Sci. (Wash.) 70, 3305–3310 (1973)

    Google Scholar 

  15. Rossmann, M. G.: The molecular replacement method. A collection of papers on the use of noncrystallographic symmetry (M. G. Rossmann, ed.). New York, London, Paris: Gordon and Breach, Science publishers 1972

    Google Scholar 

  16. Schiechl, H., Hilschmann, N.: Die PrimÄrstruktur einer monoklonalen Immunglobulin-L-Kette der Subgruppe I vom χ-Typ (Bence-Jones Protein Au): gekoppelte Austausche innerhalb der Subgruppen. Hoppe-Seylers Z. physiol. Chem. 352, 111–115 (1971)

    Google Scholar 

  17. Schiffer, M., Girling, R. L., Ely, K. R., Edmundson, A. B.: Structure of a λ-type Bence-Jones protein at 3.5 å resolution. Biochemistry 12, 4620–4631 (1973)

    Google Scholar 

  18. Schramm, H. J.: Die Isolation und Kristallisation des variablen Fragments eines Bence-Jones Proteins. Hoppe-Seylers Z. physiol. Chem. 352, 1134–1138 (1971)

    Google Scholar 

  19. Schramm, H. J., Steigemann, W., Schwager, P., Huber, R., Hoppe, W.: Crystallisation and X-ray investigation of immunglobulin-fragments. Immunochemistry 7, 872 (1970)

    Google Scholar 

  20. Segal, D. M., Padlan, E. A., Cohen, G. H., Rudikoff, S., Potter, M., Davies, D. R.: The three-dimensional structure of a phosphoryl-choline-binding mouse immunoglobulin fab and the nature of the antigen binding site. Proc. nat. Acad. Sci. (Wash.) (1974) (in press)

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Extract from Dissertation, München (1974).

on leave from the Division of Biological and Medical Research, Argonne National Laboratory, Argonne, Illinois 60439, USA.

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Fehlhammer, H., Schiffer, M., Epp, O. et al. The structure determination of the variable portion of the Bence-Jones protein Au. Biophys. Struct. Mechanism 1, 139–146 (1975). https://doi.org/10.1007/BF00539775

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Key words

  • Immunoglobulin
  • Bence-Jones
  • X-Ray
  • Structure
  • Rotation-Function
  • Patterson Search
  • Translation Function
  • Molecular Replacement