| Primary Identifier | IPR034059 | Type | Domain |
| Short Name | TNFRSF_N_viral |
| description | Viral TNFR homologues include vaccinia virus (VACV) cytokine response modifier E (CrmE) [], an encoded TNFR that shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75, TNFR type 2) [], a cowpox virus encoded cytokine-response modifier B (CrmB) [], which is a secreted form of TNF receptor that can contribute to the modification of TNF-mediated antiviral processes, and a myxoma virus (MYXV) T2 (M-T2) protein that binds and inhibits rabbit TNF-alpha []. The CrmE structure confirms that the canonical TNFR fold is adopted, but only one of the two "ligand-binding"loops of TNFRSF1A is conserved, suggesting a mechanism for the higher affinity of poxvirusTNFRs for TNFalpha over lymphotoxin-alpha []. CrmB protein specifically binds TNF-alpha and TNF-beta indicating that cowpox virus seeks to invade antiviral processes mediated by TNF. Intracellular M-T2 blocks virus-induced lymphocyte apoptosis via a highly conserved viral preligand assembly domain (vPLAD), which controls receptor signaling competency prior to ligand binding [].This entry represents the N-terminal domain of viral TNFRs. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ]. |
