Intrinsic ligand binding properties of the human and bovine α,‐interferon receptors
- 22 August 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 350 (2-3) , 281-286
- https://doi.org/10.1016/0014-5793(94)00787-x
Abstract
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.Keywords
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