TI  - cDNA cloning and characterization of the human <prot><prot><prot>interleukin 13</prot> receptor</prot>
      alpha chain</prot>.
PG  - 29265-70
AB  - We have cloned cDNAs corresponding to the human <prot><prot><prot>interleukin 13</prot> receptor</prot>
      alpha chain</prot> (<prot>IL-13Ralpha</prot>). The protein has 76% homology to murine
      <prot>IL-13Ralpha</prot>, with 95% amino acid identity in the cytoplasmic domain. Only
      weak  <prot>IL-13</prot>  binding activity was found in cells transfected with only
       <prot>IL-13Ralpha</prot> ; however, the combination of both  <prot>IL-13Ralpha</prot>  and  <prot>IL-4Ralpha</prot> 
      resulted in substantial binding activity, with a Kd of approximately 400
      pM, indicating that both chains are essential components of the   <prot><prot>IL-13</prot>  
      receptor</prot>. Whereas <prot>IL-13Ralpha</prot> serves as an alternative accessory protein
      to the common <prot>cytokine receptor gamma chain</prot> (<prot>gammac</prot>) for <prot>IL-4</prot> signaling,
      it could not replace the function of <prot>gammac</prot> in allowing enhanced <prot>IL-2</prot>
      binding activity. Nevertheless, the overall size and length of the
      cytoplasmic domain of <prot>IL-13Ralpha</prot> and <prot>gammac</prot> are similar, and like <prot>gammac</prot>,
      <prot>IL-13Ralpha</prot> is located on chromosome X.
AD  - Laboratory of Molecular Immunology, NHLBI, National Institutes of Health,
