Primary Identifier | IPR001368 | Type | Domain |
Short Name | TNFR/NGFR_Cys_rich_reg |
description | A number of proteins, some of which are known to be receptors for growth factors, have been found to contain a cysteine-rich domain of about 110 to 160 amino acids in their N-terminal part, that can be subdivided into four (or in some cases, three) modules of about 40 residues containing 6 conserved cysteines. Some of the proteins containing this domain are listed below [, , ]:Tumor Necrosis Factor type I and type II receptors (TNFR). Both receptors bind TNF-alpha and TNF-beta, but are only similar in the cysteine-rich region. TNFR contains four cysteine-rich domain modules (CRDs), termed CRD1 through CRD4. CRD2 and CRD3 are known as TNF-binding domains [].Shope fibroma virus soluble TNF receptor (protein T2)Lymphotoxin alpha/beta receptorLow-affinity nerve growth factor receptor (LA-NGFR) (p75)CD40 (Bp50), the receptor for the CD40L (or TRAP) cytokineCD27, the receptor for the CD27L cytokineCD30, the receptor for the CD30L cytokineT-cell protein 4-1BB, the receptor for the 4-1BBL putative cytokine FAS antigen (or APO-1), the receptor for FASL, a protein involved in apoptosis (programmed cell death)T-cell antigen OX40, the receptor for the OX40L cytokineWsl-1, a receptor (for a yet undefined ligand) that mediates apoptosisVaccinia virus protein A53 (SalF19R)It has been shown []that the six cysteines all involved in intrachaindisulphide bonds. A schematic representation of the structure of the 40 residuemodule of these receptors is shown below:+-------------+ +--------------+| | | |xCxxxxxxxxxxxxxCxCxxCxxxxxxxxxCxxxxCxx| |+------------+'C': conserved cysteine involved in a disulphide bond. |