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Chimeric interferon-gamma receptors demonstrate that an accessory factor required for activity interacts with the extracellular domain.

作者信息

Hibino Y, Kumar C S, Mariano T M, Lai D H, Pestka S

机构信息

Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854-5635.

出版信息

J Biol Chem. 1992 Feb 25;267(6):3741-9.

PMID:1531478
Abstract

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.

摘要

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