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 receptor 8 (also known as CD30 and Ki-1 antigen) was originally described as a marker of Hodgkin's and Reed-Sternberg cells in Hodgkin's lymphoma. Expression of the receptor is largely restricted to virus-infected lymphocytes, neoplasms of lymphoid origin and a subset of activated T cells that produce Th2-type cytokines. The receptor has pleiotropic biological functions, including inducement apoptosis and enhancement of cell survival.