The 126Gln of human interleukin-2 (IL-2) is a conserved amino acid res
idue. After substitution of 126Gln with Asp, the binding abilities of
this mutant to different composites of IL-2 receptor (R) subunits have
been determined. Results show that 126Asp-IL-2 has higher affinity to
IL-2R alpha beta gamma complex and normal affinity to IL-2R alpha bet
a complex, but loses its binding ability to IL-2R beta gamma complex,
demonstrating that the 126Gln is the residue of human IL-2 which binds
to IL-2R gamma subunit.