| First Author | Novick D | Year | 1994 |
| Journal | Cell | Volume | 77 |
| Issue | 3 | Pages | 391-400 |
| PubMed ID | 8181059 | Mgi Jnum | J:36002 |
| Mgi Id | MGI:83444 | Doi | 10.1016/0092-8674(94)90154-6 |
| Citation | Novick D, et al. (1994) The human interferon alpha/beta receptor: characterization and molecular cloning. Cell 77(3):391-400 |
| abstractText | We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs). A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced. Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2. The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits. We isolated and expressed a 1.5 kb cDNA, coding for the IFN-alpha/beta receptor. Its 331 amino acid sequence includes a leader and a transmembrane region, while its ectodomain corresponds to p40. IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction. |
