Description
The functional IL-10 receptor consists of two polypeptide chains, a ligand binding chain IL-10 Rα (IL-10 R1) and a signal transduction molecule known as IL-10 Rβ (IL-10 R2). Both chains of the IL-10 Rare expressed on many hematopoietic cells, including lymphocytes, monocytes and neutrophils, with the IL-10 Rβ chain expressed at higher levels than the IL-10 Rα chain in most cases. Interleukin 10 receptor beta (IL-10 Rβ), also known as CD210b and CRF2-4, is an 80-85 kDa member of the type II cytokine receptor family of proteins and contains two fibronectin type-III domains. The widely expressed IL-10 Rβ serves as a signal transducing accessory chain not only for IL-10, but also for other interleukins including IL-22, -28A, -28B and -29 (plus IL-26 in human) when complexed to the ligand-binding chains. It has been shown that the action of IL-10 delivered through its receptor can affect a variety of immune functions including inhibition of proinflammatory cytokine synthesis and regulation of the growth and function of B cells and antigen presenting cells. The human IL-10 Rβ shares 69% homology to its mouse counterpart in amino acid sequence. Research evidences indicated that defects in IL10RB are associated with susceptibility to hepatitis B virus infection