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. 2000 Jul 25;97(16):8991–8996. doi: 10.1073/pnas.160130297

Figure 5.

Figure 5

A model of Tyk2 regulation in the IFNα receptor-kinase complex. Tyk2 is associated with IFNAR1 through its N region. The KL domain maintains the TK domain in an unphosphorylated and resting conformation. Severe disruption of KL leads to hyperphosphorylation of the protein. Upon IFNα binding, KL-dependent conformational changes allow transition of the receptor-kinase complex to a high-affinity binding state where Tyk2 and JAK1 are stabilized in their activated conformations.