| Description | Interferon (IFN)-gamma is a dimeric glycoprotein produced by activated T cells and natural killer cells. Although originally isolated based on its antiviral activity, IFN-gamma also displays powerful anti-proliferative and immunomodulatory activities, which are essential for developing appropriate cellular defences against a variety of infectious agents. The first step in eliciting these responses is the specific high affinity interaction of IFN-gamma with its cell-surface receptor (IFN-gammaRalpha); the complex then interacts with at least one of a family of additional species-specific accessory factors (AF-1 or IFN-gammabeta), which convey different cellular responses. One such response is the association and phosphorylation of two protein tyrosine kinases (Jak-1 and Jak-2), which in turn stimulate nuclear transcription activators [].This entry includes:The human IFN-gamma receptor 1 (IFN-gammaR1), a member of the hematopoietic cytokine receptor superfamily. It is expressed in a membrane-bound form in many cell types, and is over-expressed in tumour cells. It comprises an extracellular portion of 229 residues, a single transmembrane region, and a cytoplasmic domain of 221 residues. As with other members of its superfamily, the cytokine-binding sites are formed by a small set of closely-spaced surface loops that extend from a β-sheet core, much like antigen-binding sites on antibodies. The extracellular IFN-gammaR monomer comprises two domains (D1 and D2 domains), each resembling an Ig-like fold with fibronectin type III topology [ , , ]. The signalling complex comprises two IFN-gammaR1 chains and two IFN-gammaR2 chains, which dimerises in an IFN-gamma-driven fashion [].The vaccinia virus interferon (IFN)-gamma receptor (IFN-gammaR) is a 43kDa soluble glycoprotein that is secreted from infected cells early during infection. IFN-gammaR from vaccinia virus, cowpoxvirus and camelpox virus exist naturally as homodimers, whereas the cellular IFN-gammaR dimerizes only upon binding the homodimeric IFN-gamma. The existence of the virus protein as a dimer in the absence of ligand may provide an advantage to the virus in efficient binding and inhibition of IFN-gamma in solution [ ].This is the D2 domain, which is involved in forming receptor-receptor contacts [ ]. | Name | Interferon gamma receptor, D2 domain, poxvirus/mammal |
| Short Name | IFN_gamma_rc_D2_pox/mammal | Type | Domain |
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