Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

Structure at 4.5 Å; Resolution of a Phosphorylcholine-binding Fab

Nature New Biology volume 245, pages 165–167 (1973)Cite this article

Abstract

The electron density at 4.5 Å resolution of the Fab' fragment of McPC603 mouse myeloma immunoglobulin with phosphorylcholine-binding activity can be divided into four distinct globular regions which are interpreted to correspond to the four domains in the molecule. The hapten-binding site was located by difference Fourier techniques and lies between two domains near one end of the molecule.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Sarma, V. R., Silverton, E. W., Davies, D. R., and Terry, W. D., J. biol. Chem., 246, 3753 (1971).

    CAS  PubMed  Google Scholar 

  2. Poljak, R. J., Amzel, L. M., Avey, H. P., Becka, L. N., and Nisonoff, A., Nature new Biol., 235, 137 (1972).

    Article  CAS  Google Scholar 

  3. Potter, M., Physiol. Rev., 52, 631 (1972).

    Article  CAS  Google Scholar 

  4. Inbar, D., Rotman, M., and Givol, D., J. biol. Chem., 246, 6272 (1971).

    CAS  PubMed  Google Scholar 

  5. Rudikoff, S., Potter, M., Segal, D. M., Padlan, E. A., and Davies, D. R., Proc. natn. Acad. Sci. U.S.A., 69, 3689 (1972).

    Article  CAS  Google Scholar 

  6. Bokhoven, C., Schoone, J. C., and Bijvoot, J. M., Acta Cryst., 4, 275 (1951).

    Article  CAS  Google Scholar 

  7. Dickerson, R. E., Kendrew, J. C., and Strandberg, B. E., Acta Cryst., 14, 1188 (1961).

    Article  CAS  Google Scholar 

  8. Edelman, G. M., and Gall, W. E., A. Rev. Biochem., 38, 415 (1969).

    Article  CAS  Google Scholar 

  9. Muirhead, H., Cox, J. M., Mazarella, L., and Perutz, M. F., J. molec. Biol, 28, 117 (1967).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratories of Molecular Biology and Chemistry, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland, 20014

    E. A. PADLAN, D. M. SEGAL & T. F. SPANDE

  2. Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20014

    D. R. DAVIES, S. RUDIKOFF & M. POTTER

Authors
  1. E. A. PADLAN
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. D. M. SEGAL
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. T. F. SPANDE
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. D. R. DAVIES
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. S. RUDIKOFF
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. M. POTTER
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

PADLAN, E., SEGAL, D., SPANDE, T. et al. Structure at 4.5 Å; Resolution of a Phosphorylcholine-binding Fab. Nature New Biology 245, 165–167 (1973). https://doi.org/10.1038/newbio245165a0

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1038/newbio245165a0

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing