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:

Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor

Nature volume 372, pages 336–343 (1994)Cite this article

Abstract

The three-dimensional structure of the rat neonatal Fc receptor (FcRn) is similar to the structure of molecules of the major histocompatibility complex (MHC). The counterpart of the MHC peptide-binding site is closed in FcRn, making the FcRn groove incapable of binding peptides. A dimer of FcRn heterodimers seen in the crystals may represent a receptor dimer that forms when the Fc portion of a single immunoglobulin binds. An alternative use of the MHC fold for immune recognition is indicated by the FcRn and FcRn/Fc co-crystal structures.

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. Ravetch, J. V. Cell 78, 553–560 (1994).

    Article  CAS  Google Scholar 

  2. Rodewald, R. J. Cell Biol. 45, 635–640 (1970).

    Article  CAS  Google Scholar 

  3. Rodewald, R. J. Cell Biol. 71, 666–670 (1976).

    Article  CAS  Google Scholar 

  4. Roberts, D. M., Guenthert, M. & Rodewald, R. J. Cell Biol. 111, 1867–1876 (1990).

    Article  CAS  Google Scholar 

  5. Story, C. M., Mikulska, J. E. & Simister, N. E. J. exp. Med. 180, 2377–2381 (1994).

    Article  CAS  Google Scholar 

  6. Simister, N. E. & Mostov, K. E. Nature 337, 184–187 (1989).

    Article  ADS  CAS  Google Scholar 

  7. Ahouse, J. J. et al. J. Immun. 151, 6076–6088 (1993).

    CAS  PubMed  Google Scholar 

  8. Simister, N. E. & Rees, A. R. Eur. J. Immun. 15, 733–738 (1985).

    Article  CAS  Google Scholar 

  9. Townsend, A. & Bodmer, H. A. Rev. Immun. 7, 601–624 (1989).

    Article  CAS  Google Scholar 

  10. Bjorkman, P. J. et al. Nature 329, 506–512 (1987).

    Article  ADS  CAS  Google Scholar 

  11. Garrett, T. P. J., Saper, M. A., Bjorkman, P. J., Strominger, J. L. & Wiley, D. C. Nature 342, 692–696 (1989).

    Article  ADS  CAS  Google Scholar 

  12. Madden, D. R., Gorga, J. C., Strominger, J. L. & Wiley, D. C. Cell 70, 1035–1048 (1992).

    Article  CAS  Google Scholar 

  13. Fremont, D. H., Matsumura, M., Stura, E. A., Peterson, P. A. & Wilson, I. A. Science 257, 919–927 (1992).

    Article  ADS  CAS  Google Scholar 

  14. Zhang, W. G., Young, A. C. M., Imarai, M., Nathenson, S. G. & Sacchettini, J. C. Proc. natn. Acad. Sci. U.S.A. 89, 8403–8407 (1992).

    Article  ADS  CAS  Google Scholar 

  15. Young, A. C. M., Zhang, W., Sacchettini, J. C. & Nathenson, S. G. Cell 76, 39–50 (1994).

    Article  CAS  Google Scholar 

  16. Gastinel, L. N., Simister, N. E. & Bjorkman, P. J. Proc. natn. Acad. Sci. U.S.A. 89, 638–642 (1992).

    Article  ADS  CAS  Google Scholar 

  17. Burmeister, W. P., Huber, A. H. & Bjorkman, P. J. Nature 372, 379–383 (1994).

    Article  ADS  CAS  Google Scholar 

  18. Jones, T. A. a, yaap, asap, (a #*? A Set of Averaging Programs (SERC, Daresbury, UK, 1992).

  19. Brünger, A. T. X-PLOR (Version 3.1): A System for Crystallography and NMR (Yale University, New Haven, CT, 1992).

    Google Scholar 

  20. Hope, H. A. Rev. Biophys. biophys. Chem. 19, 107–126 (1990).

    Article  CAS  Google Scholar 

  21. Brünger, A. T. Nature 355, 472–475 (1992).

    Article  ADS  Google Scholar 

  22. Hodel, A., Kim, S.-H. & Brünger, A. T. Acta crystallogr. A48, 851–858 (1992).

    Article  Google Scholar 

  23. Raghavan, M., Gastinel, L. N. & Bjorkman, P. J. Biochemistry 32, 8654–8660 (1993).

    Article  CAS  Google Scholar 

  24. Brown, J. H. et al. Nature 364, 33–39 (1993).

    Article  ADS  CAS  Google Scholar 

  25. Davies, D. R. & Metzger, H. A. Rev. Immun. 1, 87–117 (1983).

    Article  CAS  Google Scholar 

  26. Lancet, D., Parham, P. & Strominger, J. L. Proc. natn. Acad. Sci. U.S.A. 76, 3844–3848 (1979).

    Article  ADS  CAS  Google Scholar 

  27. Saper, M. A., Bjorkman, P. J. & Wiley, D. C. J. molec. Biol. 219, 277–319 (1991).

    Article  CAS  Google Scholar 

  28. Stern, L. J. et al. Nature 368, 215–221 (1994).

    Article  ADS  CAS  Google Scholar 

  29. Matsumura, M., Fremont, D. H., Peterson, P. A. & Wilson, I. A. Science 257, 927–934 (1992).

    Article  ADS  CAS  Google Scholar 

  30. Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S. & Foeller, C. Sequences of Proteins of Immunological Interest (US Department of Health and Human Services, Bethesda, MD, 1991).

    Google Scholar 

  31. Fahnestock, M. L., Tamir, I., Narhi, L. & Bjorkman, P. J. Science 258, 1658–1662 (1992).

    Article  ADS  CAS  Google Scholar 

  32. Huber, A. H., Kelley, R. F., Gastinel, L. N. & Bjorkman, P. J. J. molec. Biol. 230, 1077–1083 (1993).

    Article  CAS  Google Scholar 

  33. Beavil, A. J. et al. Biochem. Soc. Trans. 21, 968–972 (1993).

    Article  CAS  Google Scholar 

  34. Jardetzky, T. S. et al. Nature 368, 711–718 (1994).

    Article  ADS  CAS  Google Scholar 

  35. Raghavan, M., Chen, M. Y., Gastinel, L. N. & Bjorkman, P. J. Immunity 1, 303–315 (1994).

    Article  CAS  Google Scholar 

  36. Salter, R. D. et al. Nature 345, 41–46 (1990).

    Article  ADS  CAS  Google Scholar 

  37. Deisenhofer, J. Biochemistry 20, 2361–2370 (1981).

    Article  CAS  Google Scholar 

  38. Leahy, D. J., Axel, R. & Hendrickson, W. A. Cell 68, 1145–1162 (1992).

    Article  CAS  Google Scholar 

  39. Martin, L. H., Calabi, F., Lefevre, F.-A., Bilsland, C. A. & Milstein, C. Proc. natn. Acad. Sci. U.S.A. 84, 9189–9193 (1987).

    Article  ADS  CAS  Google Scholar 

  40. Schall, S. & Barnard, E. A. J. molec. Biol. 41, 237–251 (1969).

    Article  Google Scholar 

  41. Teng, T.-Y. J. appl. Crystallogr. 23, 387–391 (1990).

    Article  CAS  Google Scholar 

  42. CCP4. The SERC (UK) Collaborative Computing Project No. 4, a Suite of Programs for Protein Crystallography (Daresbury Laboratory, Warrington WA4 4AD, UK, 1979).

  43. Otwinowski, Z. in Isomorphous Replacement and Anomalous Scattering 80–86 (Daresbury Laboratory, UK, 1991).

    Google Scholar 

  44. Leslie, A. G. W. Acta crystallogr. A43, 134–136 (1987).

    Article  Google Scholar 

  45. Jones, T. A., Bergdoll, M. & Kjeldgaard, M. Crystallographic Computing and Modeling Methods in Molecular Design (Springer, New York, 1993).

    Google Scholar 

  46. Brünger, A. T. Acta crystallogr. A46, 46–57 (1990).

    Article  Google Scholar 

  47. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1991).

    Article  Google Scholar 

  48. Kraulis, P. J. J. appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

  49. Nicholls, A., Sharp, K. A. & Honig, B. Protein Struct. Funct. Genet. 11, 281–296 (1991).

    Article  CAS  Google Scholar 

  50. Evans, S. V. J. molec. Graph. 4, 134–138 (1993).

    Article  Google Scholar 

Download references

Author information

Author notes

  1. Louis N. Gastinel

    Present address: Agouron Pharmaceuticals Inc., 3565 General Atomics Court, San Diego, CA, 92121, USA

  2. Michael L. Blum

    Present address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA, 02115, USA

  3. Pamela J. Bjorkman: To whom correspondence should be addressed.

Authors and Affiliations

  1. Division of Biology 156-29, California Institute of Technology, Pasadena, California, 91125, USA

    Wilhelm P. Burmeister, Louis N. Gastinel, Michael L. Blum & Pamela J. Bjorkman

  2. Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California, 91125, USA

    Louis N. Gastinel & Pamela J. Bjorkman

  3. Biology Department and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02254, USA

    Neil E. Simister

Authors
  1. Wilhelm P. Burmeister
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Louis N. Gastinel
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Neil E. Simister
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Michael L. Blum
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Pamela J. Bjorkman
    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

Burmeister, W., Gastinel, L., Simister, N. et al. Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature 372, 336–343 (1994). https://doi.org/10.1038/372336a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/372336a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

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