Both interleukin-2 (IL-2) receptor gamma subunit and non-receptor tyrosine
kinase Jak3 play important roles in IL-2 physiological functions. Jak3 has
been known to bind IL-2R gamma and the interaction is very important for IL
-2 signaling. In order to find the domains directly involved in the interac
tion between IL-2R gamma and Jak3, various deletion mutants have been const
ructed and their interaction has been studied using the yeast two-hybrid sy
stem. Results show that the JH3-JH7 region of Jak3 N-terminal can bind to i
ntracellular domain of IL-2R gamma directly and the intact structure of JH3
-JH7 region is necessary for this combination. In addition, the region from
305 to 317 amino acid residues near the C-terminal of IL-2R gamma plays a
critical role in this interaction