[go: up one dir, main page]
More Web Proxy on the site http://driver.im/
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 of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide

Nature volume 368, pages 215–221 (1994)Cite this article

Abstract

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

Access through your institution
Buy or subscribe

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

Access options

Access through your institution

Buy this article

  • Purchase on SpringerLink
  • 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. Jorgensen, J. L., Reay, P. A., Ehrich, E. W. & Davis, M. M. A. Rev. Immun. 10, 835–873 (1992).

    Article  CAS  Google Scholar 

  2. Germain, R. N. & Margulies, D. H. A. Rev. Immun. 11, 403–450 (1993).

    Article  CAS  Google Scholar 

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

    Article  ADS  CAS  PubMed  Google Scholar 

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

    Article  ADS  CAS  PubMed  Google Scholar 

  5. Falk, K., Rötzschke, O., Stevanovic, S., Jung, G. & Rammensee, H.-G. Nature 351, 290–296 (1991).

    Article  ADS  CAS  PubMed  Google Scholar 

  6. Hunt, D. F. et al. Science 255, 1261–1263 (1992).

    Article  ADS  CAS  PubMed  Google Scholar 

  7. Jardetzky, T. S., Lane, W. S., Robinson, R. A., Madden, D. R. & Wiley, D. C. Nature 253, 326–329 (1991).

    Article  ADS  Google Scholar 

  8. Rudensky, A. Y., Preston-Hurlburt, P., Al-Ramadi, B. K., Rothbard, J. & Janeway, C. A. J. Nature 359, 429–431 (1992).

    Article  ADS  CAS  PubMed  Google Scholar 

  9. Chicz, R. M. et al. Nature 358, 764–768 (1992).

    Article  ADS  CAS  PubMed  Google Scholar 

  10. Hammer, J. et al. Cell 74, 197–203 (1993).

    Article  CAS  PubMed  Google Scholar 

  11. Sette, A. et al. J. Immun. 151, 3163–3170 (1993).

    CAS  PubMed  Google Scholar 

  12. Madden, D. R., Gorga, J. C., Strominger, J. L. & Wiley, D. C. Nature 353, 321–325 (1991).

    Article  ADS  CAS  PubMed  Google Scholar 

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

    Article  CAS  PubMed  Google Scholar 

  14. Silver, M. L., Guo, H.-C., Strominger, J. L. & Wiley, D. C. Nature 360, 367–369 (1992).

    Article  ADS  CAS  PubMed  Google Scholar 

  15. Madden, D. R., Garboczi, D. N. & Wiley, D. C. Cell 75, 693–708 (1993).

    Article  CAS  PubMed  Google Scholar 

  16. Zhang, W., 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 

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

    Article  ADS  CAS  PubMed  Google Scholar 

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

    Article  CAS  PubMed  Google Scholar 

  19. Madden, D. R. & Wiley, D. C. Curr. Opin. Struct. Biol. 2, 300–304 (1992).

    Article  CAS  Google Scholar 

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

    Article  ADS  CAS  PubMed  Google Scholar 

  21. Guo, H.-C. et al. Proc. natn. Acad. Sci. U.S.A. 90, 8053–8057 (1993).

    Article  ADS  CAS  Google Scholar 

  22. Jardetzky, T. S. et al. EMBO J. 9, 1797–1803 (1990).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Rothbard, J. B. & Gefter, M. L. A. Rev. of Immun. 9, 527–565 (1991).

    Article  CAS  Google Scholar 

  24. Stern, L. J. & Wiley, D. C. Cell 68, 465–477 (1992).

    Article  CAS  PubMed  Google Scholar 

  25. Alexander, J. et al. J. Immun. 150, 1–7 (1993).

    CAS  PubMed  Google Scholar 

  26. O'Sullivan, D. et al. J. Immun. 147, 2663–2669 (1991).

    CAS  PubMed  Google Scholar 

  27. O'Sullivan, D., Sidney, J., del Guercio, M.-F., Colòn, S. M. & Sette, A. J. Immun. 146, 1240–1246 (1991).

    CAS  PubMed  Google Scholar 

  28. Lee, B. & Richards, F. M. J. molec. Biol. 55, 379–400 (1971).

    Article  CAS  PubMed  Google Scholar 

  29. Brown, J. H. et al. Nature 332, 845–850 (1988).

    Article  ADS  CAS  PubMed  Google Scholar 

  30. Le Questel, J.-Y., Morris, D. G., Maccallum, P. H., Peot, R. & Milner-White, E. J. J. molec. Biol. 231, 888–896 (1993).

    Article  CAS  PubMed  Google Scholar 

  31. Hammer, J., Takacs, B. & Sinigaglia, F. J. exp. Mec. 176, 1007–1013 (1992).

    Article  CAS  Google Scholar 

  32. Demotz, S., Barbey, C., Corradin, G., Amoroso, A. & Lanzavecchia, A. Eur. J. Immun. 23, 425–432 (1993).

    Article  CAS  Google Scholar 

  33. Verreck, F. A. W., Termijtelen, A. & Konig, F. Eur. J. Immun. 23, 1346–1350 (1992).

    Article  Google Scholar 

  34. Newton-Nash, D. K. & Eckels, D. D. J. Immun. 150, 1813–1821 (1993).

    CAS  PubMed  Google Scholar 

  35. Busch, R., Hill, C. M., Hayball, J. D., Lamb, J. R. & Rothbard, J. B. J. Immun. 147, 1292–1298 (1991).

    CAS  PubMed  Google Scholar 

  36. Boehncke, W.-H. et al. J. Immun. 150, 331–341 (1993).

    CAS  PubMed  Google Scholar 

  37. Geluk, A. et al. J. Immun. 149, 2864–2871 (1992).

    CAS  PubMed  Google Scholar 

  38. Malcherek, G. et al. Int. Immun. 5, 1229–1237 (1993).

    Article  CAS  PubMed  Google Scholar 

  39. Kreiger, J. I. et al. J. Immun. 146, 2331–2340 (1991).

    Google Scholar 

  40. Coppin, H. L. et al. Eur. J. Immun. 23, 343–349 (1993).

    Article  CAS  Google Scholar 

  41. Ong, B. et al. Proc. natn. Acad. Sci. U.S.A. 88, 7343–7347 (1991).

    Article  ADS  CAS  Google Scholar 

  42. Olsen, A. C. et al. Eur. J. Immun. (in the press).

  43. Driscoll, P. C. et al. J. molec Biol. 232, 342–350 (1993).

    Article  CAS  PubMed  Google Scholar 

  44. Fitzgerald, P. M. D. J. appl. Crystallogr. 21, 273–278 (1988).

    Article  CAS  Google Scholar 

  45. Bricogne, G. Acta crystallogr. A32 832–847 (1976).

    Article  Google Scholar 

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

    Article  Google Scholar 

  47. Brünger, A. T. X-PLOR (Version 3.1): A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, 1992).

    Google Scholar 

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

    Article  Google Scholar 

  49. Carson, M. J. molec. Graphics 5, 103–106 (1987).

    Article  CAS  Google Scholar 

  50. Connolly, M. L. J. appl. Crystallogr. 16, 548–558 (1983).

    Article  CAS  Google Scholar 

  51. Luzzati, V. Acta crystallogr. 5, 802–811 (1952).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Robert G. Urban & Jack L. Strominger

  2. Howard Hughes Medical Institute, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Lawrence J. Stern, Theodore S. Jardetzky & Don C. Wiley

  3. Rosenstiel Research Center, Brandeis University, 415 South Street, Waltham, Massachusetts, 02254, USA

    Jerry H. Brown

  4. Rangos Research Center, Children's Hospital of Pittsburgh and University of Pittsburgh Medical Center, 3705 Fifth Avenue, Pittsburgh, Pennsylvania, 15213, USA

    Joan C. Gorga

Authors
  1. Lawrence J. Stern
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jerry H. Brown
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Theodore S. Jardetzky
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Joan C. Gorga
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Robert G. Urban
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Jack L. Strominger
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Don C. Wiley
    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

Stern, L., Brown, J., Jardetzky, T. et al. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368, 215–221 (1994). https://doi.org/10.1038/368215a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/368215a0

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