interleukin-10 receptor binding

Definition

Target type: molecularfunction

Binding to an interleukin-10 receptor. [GOC:ai]

Interleukin-10 receptor (IL-10R) binding is a crucial step in the signaling pathway initiated by the cytokine interleukin-10 (IL-10). IL-10 is a potent immunosuppressive cytokine that plays a critical role in regulating immune homeostasis and preventing excessive inflammation. Its ability to suppress immune responses is primarily mediated through its interaction with the IL-10R complex on target cells. The IL-10R complex is composed of two subunits: IL-10Rα and IL-10Rβ. IL-10 binds to IL-10Rα with high affinity, inducing a conformational change that facilitates the recruitment of IL-10Rβ. This heterodimerization of the receptor subunits initiates downstream signaling events. Upon binding of IL-10, the IL-10R complex undergoes a series of conformational changes that activate associated intracellular signaling molecules, including the Janus kinase (JAK) family of tyrosine kinases. Activated JAKs phosphorylate tyrosine residues on the cytoplasmic tails of IL-10Rα and IL-10Rβ, creating docking sites for signal transducer and activator of transcription (STAT) proteins. STAT proteins bind to the phosphorylated tyrosine residues, become phosphorylated themselves, and dimerize. These activated STAT dimers translocate to the nucleus where they bind to specific DNA sequences, known as STAT response elements, to regulate the expression of target genes. The molecular function of IL-10 receptor binding, therefore, involves a cascade of events that ultimately lead to the modulation of gene expression, resulting in the suppression of pro-inflammatory cytokine production, inhibition of T cell activation and proliferation, and promotion of immune tolerance. This precise regulation of immune responses through IL-10R binding is essential for maintaining immune homeostasis and preventing uncontrolled inflammation in the body.'
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Proteins (1)

Compounds (1)