Interleukin 10 Receptor
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Interleukin 10 Receptor
Interleukin-10 receptor (IL-10R) is a type II cytokine receptor. The receptor is tetrameric, composed of 2 α and 2 β subunits. The α subunit (encoded in the ''Il10ra gene)'' is expressed on haematopoietic cells (such as T, B, NK, mast, and dendritic cells) whilst the β subunit (encoded in the ''Il10rb gene'') is expressed ubiquitously. The α subunit is exclusive to interleukin-10, however the β subunit is shared with other type II cytokine receptors such as IL-22R, IL-26R and INFλR. The IL-10R α subunit acts as the ligand binding site and may be upregulated in various cell types as necessary. The IL-10R β functions as the signaling subunit and is constitutively expressed in a majority of cell types. There is evidence that upon ligand binding at the α subunit, a conformational change occurs in the β subunit that allows it to additionally bind to IL-10. This structure forms a heterotetramer that leads to the signaling complex activation of JAK1 and TYK2 kinase ...
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Interleukin 10 Receptor, Alpha Subunit
Interleukin-10 receptor subunit alpha is a Protein subunit, subunit for the interleukin-10 receptor. ''IL10RA'' is its human gene. IL10RA has also been designated CDw210a (cluster of differentiation w210a). Function The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of myeloid progenitor cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 Protein kinase, kinases. Interactions Interleukin 10 receptor, alpha subunit has been shown to Protein-protein interaction, interact with: * Interleukin 10 and * Janus kinase 1. References Further reading

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Interleukin 10 Receptor, Beta Subunit
Interleukin 10 receptor, beta subunit is a subunit for the interleukin-10 receptor. IL10RB is its human gene. IL10RB has also been designated CDw210b (cluster of differentiation w210b). The protein encoded by this gene belongs to the cytokine receptor family. It is an accessory chain essential for the active interleukin 10 receptor complex. Coexpression of this and IL10RA proteins has been shown to be required for IL10-induced signal transduction. This gene and three other interferon receptor genes, ''IFNAR2'', ''IFNAR1 Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the ''IFNAR1'' gene. Function The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for type I interfer ...'', and '' IFNGR2'', form a class II cytokine receptor gene cluster located in a small region on chromosome 21. References Further reading * * * * * * * * * * * * * * * * * * * * Clusters of different ...
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Type II Cytokine Receptor
Type II cytokine receptors, also commonly known as class II cytokine receptors, are transmembrane proteins that are expressed on the surface of certain cells. They bind and respond to a select group of cytokines including interferon type I, interferon type II, interferon type III. and members of the interleukin-10 family These receptors are characterized by the lack of a WSXWS motif which differentiates them from type I cytokine receptors. Structure Typically type II cytokine receptors are heterodimers or multimers with a high and a low affinity component. These receptors are related predominantly by sequence similarities in their extracellular portions that are composed of tandem Ig-like domains. The structures for the extracellular domains of the receptors for interferon types, I, II, and III are all known. Type II cytokine receptors are tyrosine-kinase-linked receptors. The intracellular domain of type II cytokine receptors is typically associated with a tyrosine kina ...
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Tetrameric Protein
A tetrameric protein is a protein with a quaternary structure of four subunits (tetrameric). Homotetramers have four identical subunits (such as glutathione S-transferase), and heterotetramers are complexes of different subunits. A tetramer can be assembled as dimer of dimers with two homodimer subunits (such as sorbitol dehydrogenase), or two heterodimer subunits (such as hemoglobin). Subunit interactions in tetramers The interactions between subunits forming a tetramer is primarily determined by non covalent interaction. Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits. For homotetrameric proteins such as sorbitol dehydrogenase (SDH), the structure is believed to have evolved going from a monomeric to a dimeric and finally a tetrameric structure in evolution. The binding process in SDH and many other tetrameric enzymes can be described by the gain in free energy which can be determined ...
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Dendritic Cell
A dendritic cell (DC) is an antigen-presenting cell (also known as an ''accessory cell'') of the mammalian immune system. A DC's main function is to process antigen material and present it on the cell surface to the T cells of the immune system. They act as messengers between the innate and adaptive immune systems. Dendritic cells are present in tissues that are in contact with the body's external environment, such as the skin, and the inner lining of the nose, lungs, stomach and intestines. They can also be found in an immature and mature state in the blood. Once activated, they migrate to the lymph nodes, where they interact with T cells and B cells to initiate and shape the adaptive immune response. At certain development stages they grow branched projections, the '' dendrites,'' that give the cell its name (δένδρον or déndron being Greek for 'tree'). While similar in appearance to the dendrites of neurons, these are structures distinct from them. Immature dendr ...
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Interleukin 10
Interleukin 10 (IL-10), also known as human cytokine synthesis inhibitory factor (CSIF), is an anti- inflammatory cytokine. In humans, interleukin 10 is encoded by the ''IL10'' gene. IL-10 signals through a receptor complex consisting of two IL-10 receptor-1 and two IL-10 receptor-2 proteins. Consequently, the functional receptor consists of four IL-10 receptor molecules. IL-10 binding induces STAT3 signalling via the phosphorylation of the cytoplasmic tails of IL-10 receptor 1 + IL-10 receptor 2 by JAK1 and TYK2 respectively. Gene and protein structure The IL-10 protein is a homodimer; each of its subunits is 178- amino-acid long. IL-10 is classified as a class-2 cytokine, a set of cytokines including IL-19, IL-20, IL-22, IL-24 (Mda-7), IL-26 and interferons type-I ( IFN-alpha, -beta, -epsilon, -kappa, -omega), type-II (IFN-gamma) and type-III (IFN-lambda, including IL-28A, IL-28B, IL-29, and IFNL4). Expression and synthesis In humans, IL-10 is encoded by ...
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Type II Cytokine Receptor
Type II cytokine receptors, also commonly known as class II cytokine receptors, are transmembrane proteins that are expressed on the surface of certain cells. They bind and respond to a select group of cytokines including interferon type I, interferon type II, interferon type III. and members of the interleukin-10 family These receptors are characterized by the lack of a WSXWS motif which differentiates them from type I cytokine receptors. Structure Typically type II cytokine receptors are heterodimers or multimers with a high and a low affinity component. These receptors are related predominantly by sequence similarities in their extracellular portions that are composed of tandem Ig-like domains. The structures for the extracellular domains of the receptors for interferon types, I, II, and III are all known. Type II cytokine receptors are tyrosine-kinase-linked receptors. The intracellular domain of type II cytokine receptors is typically associated with a tyrosine kina ...
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Interleukin-22 Receptor
Interleukin-22 receptor is a type II cytokine receptor Type II cytokine receptors, also commonly known as class II cytokine receptors, are transmembrane proteins that are expressed on the surface of certain cells. They bind and respond to a select group of cytokines including interferon type I, i .... It binds to Interleukin-22. It is a heterodimer of α1 and IL-10Rβ2 subunits. References External links * Type II cytokine receptors {{membrane-protein-stub ...
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Interleukin 26
Interleukin-26 (IL-26) is a protein that in humans is encoded by the ''IL26'' gene. IL-26 is the most recently identified member of the IL-20 cytokine subfamily, which was formed according to the usage of common receptor subunits and similarities in target-cell profiles and functions. All cytokines belonging to this subfamily are members of the larger IL-10 family. IL-26 is expressed in certain herpesvirus-transformed T cells but not in primary stimulated T cells. IL-26 signals through a receptor complex comprising two distinct proteins called IL-20 receptor 1 and IL-10 receptor 2. By signaling through this receptor complex, IL-26 induces rapid phosphorylation of the transcription factors STAT1 and STAT3, which enhance IL-10 and IL-8 secretion and as expression of the CD54 molecule on the surface of epithelial cells. Gene organization and protein structure The ''IL26'' gene is conserved in various vertebrates, but it is curiously absent in mice and rats. Paralogs of this g ...
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Heterotetramer
A tetrameric protein is a protein with a quaternary structure of four subunits (tetrameric). Homotetramers have four identical subunits (such as glutathione S-transferase), and heterotetramers are complexes of different subunits. A tetramer can be assembled as dimer of dimers with two homodimer subunits (such as sorbitol dehydrogenase), or two heterodimer subunits (such as hemoglobin). Subunit interactions in tetramers The interactions between subunits forming a tetramer is primarily determined by non covalent interaction. Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits. For homotetrameric proteins such as sorbitol dehydrogenase (SDH), the structure is believed to have evolved going from a monomeric to a dimeric and finally a tetrameric structure in evolution. The binding process in SDH and many other tetrameric enzymes can be described by the gain in free energy which can be det ...
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TYK2
Non-receptor tyrosine-protein kinase TYK2 is an enzyme that in humans is encoded by the ''TYK2'' gene. TYK2 was the first member of the Janus kinase, JAK family that was described (the other members are Janus kinase 1, JAK1, Janus kinase 2, JAK2, and Janus kinase 3, JAK3). It has been implicated in interferon, IFN-α, Interleukin 6, IL-6, Interleukin 10, IL-10 and Interleukin 12, IL-12 signaling. Function This gene encodes a member of the tyrosine kinase and, to be more specific, the Janus kinases (JAKs) protein families. This protein associates with the cytoplasmic domain of type I and type II cytokine receptors and promulgate cytokine signals by phosphorylating receptor subunits. It is also component of both the type I and type III interferon signaling pathways. As such, it may play a role in anti-viral immunity. Cytokines play pivotal roles in immunity and inflammation by regulating the survival, proliferation, differentiation, and function of immune cells, as well as cell ...
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