Intrinsic ligand binding properties of the human and bovine α,‐interferon receptors

FEBS Letters

Langer, Jerome A.¹  Lim, Jin-kyu²  Xiong, Jingwei¹  Carrasco, Nancy¹ 

[1] Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA;Department of Molecular Genetics & Microbiology, UDMNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA

关键词: Interferon α receptor;    Interferon α;    Xenopus laevis oocyte;    IFN-α;    interferon alpha;    IFN-αR;    Type I IFN-α receptor;    IFN-αR1;    cloned subunit of the IFN-αR;    designated as bovine (Bo-) or human (Hu-);   

DOI  :  10.1016/0014-5793(94)00787-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Type I interferon receptor (IFN-αR) interacts with all IFN-αs, IFN-β and IFN-ω, and seems to be a multisubunit receptor. To investigate the role of a cloned receptor subunit (IFN-αR1), we have examined the intrinsic ligand binding properties of the bovine and human IFN-αR1 polypeptides expressed in Xenopus laevis oocytes. Albeit with different efficiencies, Xenopus oocytes expressing either the human or bovine IFN-αR1 polypeptide exhibit significant binding and formation of crosslinked complexes with human IFN-αA and IFN-αB. Thus, the IFN-αR1 polypeptide most likely plays a direct role in ligand binding.

【 授权许可】

Unknown