| Description | Interleukin 10 (IL-10) is a secreted 17-21kDa protein that is non- glycosylated in humans but exists as a non-covalent homodimer. IL-10 is secreted by some types of T-lymphocyte, B-lymphocytes and macrophages late after antigen activation. Generally, IL-10 inhibits T-cell and natural killer cell synthesis of other cytokines at the transcriptional level, indirectly, by affecting macrophages. These cytokines include interferon-gamma, IL-2, IL-3, tumour necrosis factor and granulocyte-macrophage colony-stimulating factor (GM-CSF). The mechanism of IL-10 induced inhibition appears to involve a reduction in the abundance of the macrophage surface molecules that directly stimulate T-cells and natural killer cells. Proteins encoded by viruses such as Epstein-Barr virus and equine herpes virus show a high degree of sequence identity to IL-10. These proteins are thought to be involved in evasion of host immune responses. The IL-10 molecule is a tight dimer of 2 interpenetrating subunits that form a V-shaped structure. Each half of the structure consists of 6 α-helices (4 from 1 subunit and 2 from the other). Four of the helices form an up-up-down-down bundle, which is observed in all other helical cytokines. The overall topology resembles interferon-gamma.This entry represents a Interleukin-10 conserved site found at the second of three conserved cysteines. | Name | Interleukin-10, conserved site |
| Short Name | IL-10_CS | Type | Conserved_site |
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