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The human interleukin-3 (IL-3) receptor is a type I receptor protein with an extracellular ligand-binding domain and a transmembrane segment. The monoclonal antibody M-20 binds with high affinity to a 140-kDa transmembrane protein of cultured cells and to the CD123 molecule on human cells. To characterize the epitope recognized by M-20 and to determine whether this molecule is representative of the IL-3 receptor, we isolated a cDNA clone encoding a M-20 antigenic determinant. The corresponding protein sequence revealed that M-20 binds to a conserved region in the extracellular domain of the receptor. Moreover, it contains a putative tyrosine-rich region in its COOH-terminal half that is not present in the CD123 molecule. These results demonstrate that the M-20 antigenic determinant is located on the IL-3 receptor and that the transmembrane segment is not involved in this binding.Q:
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