The cell surface receptor for IL-4 is composed of two polypeptide proteins that span the plasma membranes. One of these proteins chains, the IL-4Rโ, binds to IL-4 with high affinity. Binding of IL-4 to the IL-4Rโ on the cell surface results in its association with a second protein. In the type I IL-
IL-16 Receptor (CD4)
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IL-10 interacts with its tetrameric receptor complex consisting of two IL-10Rโ and two IL-10Rโ chains resulting in the phosphorylation and activation of JAK1 and TYK2 kinases, which in turn phosphorylate two tyrosine residues in the intracytoplasmic parts of the IL-10Rโ chains that form docking site
The functional high-affinity IL-12 receptor is composed of at least two โ-type receptor subunits, each independently exhibiting a low affinity for IL-12. Both subunits are members of the cytokine receptor superfamily. IL-12 p40 interacts primarily with IL-12 Rโ1, while IL-12 p35 interacts primarily
Interleukin 6 (IL-6) is a pleiotropic cytokine that regulates immune reaction, hematopoiesis, and differentiation of the nervous system. The receptor for IL-6 (IL-6R) consists of two chains, namely IL-6Rโ and gp130. Both IL-6Rโ and gp130 belong to thetype I cytokine receptor superfamily. IL-6Rโ is t