Abstract
We have identified cDNAs encoding the human interleu- kin-2 (IL-2) receptor from a cDNA library constructed from HUT-102B2 cell mRNA, and have expressed them in eukaryotic cells. Based on the deduced amino acid sequence from the DNA sequence, the IL-2 receptor is initially synthesized as a preprotein of 272 amino acids and then processed to a mature form of 251 amino acids. The protein has a very short positively charged cytoplasmic region at the carboxy end of the molecule that contains potential phosphorylation sites. The protein has two potential N-linked carbohydrate addition sites and multiple potential 0-linked carbohydrate addition sites. Although the IL-2 receptor appears to be encoded by a single structural gene, there are two distinct mRNAs that encode the protein that differ in the polyaden- ylation signal used. Further, there is evidence that alternate mRNA splicing may also occur.
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Leonard, W.J. et al. (1985). Molecular Cloning and Expression of cDNAS Encoding the Human Interleukin-2 Receptor. In: Feldmann, M., Mitchison, N.A. (eds) Immune Regulation. Experimental Biology and Medicine, vol 8. Humana Press. https://doi.org/10.1007/978-1-4612-4996-2_24
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DOI: https://doi.org/10.1007/978-1-4612-4996-2_24
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