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Structure of the human class I histocompatibility antigen, HLA-A2

Nature volume 329, pages 506–512 (1987)Cite this article

Abstract

The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel β-strands topped by α-helices. A large groove between the α-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.

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Author information

Author notes

  1. P. J. Bjorkman

    Present address: Department of Medical Microbiology, Stanford University, Stanford, California, 94305, USA

  2. W. S. Bennett

    Present address: Max-Planck-Institute für Molekulare Genetik, Abteilung Wittmann, D-1000, Berlin, 33, FDR

  3. D. C. Wiley: To whom correspondence should be addressed.

Affiliations

  1. Department of Biochemistry and Molecular Biology, Harvard University, Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts, 02138, USA

    P. J. Bjorkman, M. A. Saper, B. Samraoui, W. S. Bennett, J. L. Strominger & D. C. Wiley

  2. Department of Medical Microbiology, Stanford University, Stanford, California, 94305, USA

    P. J. Bjorkman

  3. Department of Medical Microbiology, Stanford University, Stanford, California, 94305, USA

    W. S. Bennett

Authors
  1. P. J. Bjorkman
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  2. M. A. Saper
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  3. B. Samraoui
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  4. W. S. Bennett
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  5. J. L. Strominger
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  6. D. C. Wiley
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Bjorkman, P., Saper, M., Samraoui, B. et al. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329, 506–512 (1987). https://doi.org/10.1038/329506a0

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