Structure of IL12 and its receptor IL12R

Structural characteristics of IL-12 and its receptor are summarized in Table 1. The homologies to other cytokines, mainly to IL-6 and its receptor, suggest that IL-12 has evolved from a primordial cytokine and its soluble receptor. On activated T cells (human and mouse) IL-12 binding sites of high (Kd 5-50 pM), intermediate (Kd 50-200 pM) and low (Kd 2-6 nM) affinities have been identified. In bioassays IL-12 (mouse and human) is active at concentrations of about 0.1 pM. This indicates that signaling can be induced even at low receptor occupancy. Similarly, a cell line cotransfected with the two cloned hlL-12Rfi| and (32 chains exhibited binding sites of Kd 50 pM and Kj 5-10 nM and was responsive to IL-12 at 1 pM. Signal transduction induced by IL-12 in T cells was found to include activation of tyrosine kinases JAK2 and TYK2 and phosphorylation of ST ATI (mouse), STAT3 and STAT4 (mouse and human).

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