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. Proteins known to belong to this family [1,2,3,4] are listed below:
Tumor Necrosis Factor type I and type II receptors (TNFR). Both receptors
bind TNF-α and TNF-β, but are only similar in the cysteine-rich
region.
CD40 (Bp50), the receptor for the CD40L (or TRAP) cytokine.
CD27, the receptor for the CD27L cytokine.
CD30, the receptor for the CD30L cytokine.
T-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 cytokine.
Wsl-1, a receptor (for a yet undefined ligand) that mediates apoptosis.
Vaccinia virus protein A53 (SalF19R).
It has been shown [5] that the six cysteines all involved in intrachain
disulfide bonds. A schematic representation of the structure of the 40 residue
module of these receptors is shown below:
'C': conserved cysteine involved in a disulfide bond.
We have developed a signature pattern for the cysteine-rich region. It is
based mainly on the position of the six conserved cysteines in each of the
repeats. The profile spans the complete domain.
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