| First Author | Aman MJ | Year | 1996 |
| Journal | J Biol Chem | Volume | 271 |
| Issue | 46 | Pages | 29265-70 |
| PubMed ID | 8910586 | Mgi Jnum | J:36753 |
| Mgi Id | MGI:84179 | Doi | 10.1074/jbc.271.46.29265 |
| Citation | Aman MJ, et al. (1996) cDNA cloning and characterization of the human interleukin 13 receptor alpha chain. J Biol Chem 271(46):29265-70 |
| abstractText | We have cloned cDNAs corresponding to the human interleukin 13 receptor alpha chain (IL-13Ralpha). The protein has 76% homology to murine IL-13Ralpha, with 95% amino acid identity in the cytoplasmic domain. Only weak IL-13 binding activity was found in cells transfected with only IL-13Ralpha; however, the combination of both IL-13Ralpha and IL-4Ralpha resulted in substantial binding activity, with a Kd of approximately 400 pM, indicating that both chains are essential components of the IL-13 receptor. Whereas IL-13Ralpha serves as an alternative accessory protein to the common cytokine receptor gamma chain (gammac) for IL-4 signaling, it could not replace the function of gammac in allowing enhanced IL-2 binding activity. Nevertheless, the overall size and length of the cytoplasmic domain of IL-13Ralpha and gammac are similar, and like gammac, IL-13Ralpha is located on chromosome X. |
