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The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation

Nature volume 353, pages 321–325 (1991)Cite this article

Abstract

X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27 (see accompanying article1). Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.

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Author information

Author notes

  1. J. C. Gorga

    Present address: Department of Pediatrics, Children's Hospital of Pittsburgh, 6130 Rangos Research Building, 3705 Fifth Avenue, Pittsburgh, Pennsylvania, 15213, USA

Affiliations

  1. Committee on Higher Degrees in Biophysics, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    D. R. Madden

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

    D. R. Madden, J. C. Gorga, J. L. Strominger & D. C. Wiley

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

    D. C. Wiley

Authors
  1. D. R. Madden
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  2. J. C. Gorga
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  3. J. L. Strominger
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  4. D. C. Wiley
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Madden, D., Gorga, J., Strominger, J. et al. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353, 321–325 (1991). https://doi.org/10.1038/353321a0

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  • DOI: https://doi.org/10.1038/353321a0

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