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A new member of the immunoglobulin superfamily—CTLA-4

Nature volume 328, pages 267270 (16 July 1987) | Download Citation

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Abstract

The immunoglobulin superfamily is a group of proteins, each made of one or several domains sharing key structural features with either the variable (V) or the constant (C) immunoglobulin domains1,2. It includes such functionally important members as the immunoglobulins themselves, major histocompatibility complex (MHC) class I and class II and T-cell receptor (TCR) molecules. Several members of this superfamily are expressed on lymphocytes where they are membrane-bound and capable of interactions with other members of the family, thus taking part in cell–cell recognition. In screening mouse cytolytic-T-cell-derived cDNA libraries, we came across cDNA clones defining a sequence, CTLA-4, which could encode a 223-amino-acid protein clearly belonging to the immunoglobulin superfamily. It consists of one V-like domain flanked by two hydrophobic regions, one of which has a structure suggestive of membrane anchoring. CTLA-4 is mainly expressed in activated lymphocytes and is coinduced with T-cell-mediated cytotoxicity in inducible models of this process. The mouse ctla-4 gene maps to band C of chromosome 1.

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Author notes

    • Magali Roux-Dosseto

    INSERM U.119, 27, Boulevard Leï Roure, 13009 Marseille, France

    • Marie-Geneviève Mattei

    INSERM U.242, CHU Timone, 13385 Marseille Cedex 5, France

    • Magali Roux-Dosseto

    Present address: UA CNRS 1175, Faculté de Médicine Secteur Nord, 13326 Marseille Cedex 15, France

Affiliations

  1. Centre d'Immunologie INSERM-CNRS de Marseille-Luminy, Case 906, 13288 Marseille Cedex 9, France

    • Jean-François Brunet
    • , François Denizot
    • , Marie-Françoise Luciani
    • , Magali Roux-Dosseto
    • , Marie Suzan
    • , Marie-Geneviève Mattei
    •  & Pierre Golstein

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https://doi.org/10.1038/328267a0

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