Chimeric interferon-gamma receptors demonstrate that an accessory factor required for activity interacts with the extracellular domain
We determined the species specificity and function of structural domains of the interferon-gamma receptor (IFN-gamma R) by construction of human/murine chimeric IFN-gamma R cDNA clones and their expression in various cells. We demonstrate that we can reconstitute a biologically active IFN-gamma R in...
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Veröffentlicht in: | The Journal of biological chemistry 1992-02, Vol.267 (6), p.3741-3749 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | We determined the species specificity and function of structural domains of the interferon-gamma receptor (IFN-gamma R) by
construction of human/murine chimeric IFN-gamma R cDNA clones and their expression in various cells. We demonstrate that we
can reconstitute a biologically active IFN-gamma R in eukaryotic cells with chimeric receptors as long as the extracellular
domain and an accessory factor are from the same species. These results indicate that the extracellular domain of the receptor
interacts directly or indirectly with the species-specific accessory factor. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)50588-9 |