The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with an the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is presently unknown. Mutations in this gene are associated with an interleukin 2 receptor alpha deficiency.
Human IL-2RB; also known asinterleukin-2 receptor subunit beta;is the receptor for interleukin-2. IL2 receptor complex is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. IL2 receptor complex has three forms with respect to ability to bind IL2. IL-2RB is belonged to a type I membrane protein;and has a 26 residue signal peptide; a 214 residue extracellular region; a 25 residue transmembrane region and a 286 residue cytoplasmic domain. IL-2RB is the subunit critical for receptor-mediated signaling via physically or functionally coupling to other signaling molecules; such as the Jak-STAT and Src-family protein tyrosine kinase although it lacks apparent catalytic motifs.
Human IL-2RB, also known asinterleukin-2 receptor subunit beta,is the receptor for interleukin-2. IL2 receptor complex is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. IL2 receptor complex has three forms with respect to ability to bind IL2. IL-2RB is belonged to a type I membrane protein,and has a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. IL-2RB is the subunit critical for receptor-mediated signaling via physically or functionally coupling to other signaling molecules, such as the Jak-STAT and Src-family protein tyrosine kinase although it lacks apparent catalytic motifs.
The common gamma chain (γc) (or CD132); also known as interleukin-2 receptor subunit gamma or IL2RG; is a member of the type I cytokine receptor family expressed on most lymphocyte (white blood cell) populations; and its gene is found on the X-chromosome of mammals. The common gamma chain (γc) (or IL2RG); is a cytokine receptor sub-unit that is common to the receptor complexes for at least six different interleukin receptors: IL-2; IL-4; IL-7; IL-9; IL-15 and interleukin-21 receptor. It is a component of multiple cytokine receptors that are essential for lymphocyte development and function. X-linked severe combined immunodeficiency (XSCID) is a rare and potentially fatal disease caused by mutations of IL2RG; the gene encoding IL2RG. IL2RG was demonstrated to be a component of the IL-4 receptor on the basis of chemical cross-linking data; the ability of IL2RG to augment IL-4 binding affinity. The observation that IL-2R gamma is a functional component of the IL-4 receptor; together with the finding that IL-2R gamma associates with the IL-7 receptor; begins to elucidate why deficiency of this common gamma chain (gamma c) has a profound effect on lymphoid function and development; as seen in X-linked severe combined immunodeficiency.
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