Protein Domain : Tumour necrosis factor receptor 11A IPR022361

Type  Family
Description  The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern [ ]. The cysteines allow formation of an extended rod-like structure, responsible for ligand binding []. Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences [ ]. Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved [, ]. TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis [ ]. Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease []. TNF receptors 11A and 11B mediate the effects of receptor activator for NF-kappa-B ligand (RANKL), an essential osteoclast regulatory factor. The receptors have opposing effects - activation of TNF receptor 11A by RANKL promotes osteoclast differentiation [ ], while TNF receptor 11B acts as a soluble decoy receptor for the ligand, thus inhibiting differentiation []. Mutations in the TNF receptor 11A gene have been implicated in a range of bone disorders, such as expansile osteolysis, osteopetrosis, and Paget disease of bone. The receptor also has a role in immune function, vascular disease and mammary gland development [ ].
Short Name  TNFR_11A

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