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Structure of C-terminal half of two H–2 antigens from cloned mRNA

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Abstract

The classical cell-surface histocompatibility antigens (H–2 antigens in the mouse), known to have key roles in cell-to-cell recognition1, are encoded by at least three highly polymorphic genes (H–2D, K and L)2. Like their human (HLA) counterparts3, H–2 heavy chains span the cell membrane with a short C-terminal cytoplasmic region and an N-terminal extracellular stretch of about 280 amino acids. HLA antigens seem to be organized in three domains containing β-pleated sheets, with disulphide loops within the second and third domains, but the relative scarcity of material has hampered biochemical studies of the H–2 antigens4–6. We now report the sequencing of plasmids carrying H–2 cDNA as a means of inferring the amino acid sequence of the antigens, and especially of their previously poorly described C-terminal half.

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Author notes

  1. L. Rask

    Present address: Department of Cell Research, The Wallenberg Laboratory, University of Uppsala, Uppsala, Sweden

Authors and Affiliations

  1. Unité de Biologie Moléculaire du Gène, ER CNRS no. 201 and SCN INSERM no. 20, Institut Pasteur, 28 rue du Dr Roux, 75724, Paris, Cédex 15, France

    F. Brégégère, J. P. Abastado, L. Rask, J. L. Lalanne, B. Cami, G. Gachelin & P. Kourilsky

  2. European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 102 209, D-6900, Heidelberg, FRG

    S. Kvist, H. Garoff & B. Dobberstein

  3. Department of Cell Research, The Wallenberg Laboratory, University of Uppsala, Uppsala, Sweden

    K. Wiman, D. Larhammar & P. A. Peterson

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  1. F. Brégégère
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  2. J. P. Abastado
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  3. S. Kvist
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  4. L. Rask
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  5. J. L. Lalanne
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  6. H. Garoff
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  7. B. Cami
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  8. K. Wiman
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Brégégère, F., Abastado, J., Kvist, S. et al. Structure of C-terminal half of two H–2 antigens from cloned mRNA. Nature 292, 78–81 (1981). https://doi.org/10.1038/292078a0

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