Literature References | 1. ARMITAGE, R.
Tumor necrosis factor receptor superfamily members and their ligands.
CURR.OPIN.IMMUNOL. 6 407-413 (1994).
2. BANNER D., D'ARCY, A., JAMES, W., GENTZ, R., SCHOENFELD, H., BROGER, C.,
LOETSCHER, H. AND LESSLAUER, W.
Crystal structure of the soluble human 55 kD TNF receptor-human TNF-beta
complex: implications for TNF receptor activation.
CELL 73 431-445 (1993).
3. WU, H.
Assembly of post-receptor signaling complexes for the tumor necrosis factor
receptor superfamily.
ADV.PROTEIN CHEM. 68 225-279 (2004).
4. LOCKSLEY, R., KILLEEN, N. AND LENARDO, M.
The TNF and TNF Receptor Superfamilies: Integrating Mammalian Biology.
CELL 104 487-501 (2001).
5. GRAVESTEIN, L. AND BORST, J.
Tumor necrosis factor receptor family members in the immune system.
SEMIN.IMMUNOL. 10 423-434 (1998).
6. LOENEN, W.
D27 and (TNFR) relatives in the immune system: their role in health and
disease.
SEMIN.IMMUNOL. 10 417-422 (1998).
7. PATEL, D., WALLWEBER, H., YIN, J., SHRIVER, S., MARSTERS, S., GORDON, N.,
STAROVASNIK, M. AND KELLEY, R.
Engineering an APRIL-specific B cell maturation antigen.
J.BIOL.CHEM. 279 16727-16735 (2004).
8. LAABI, Y., GRAS, M., BROUET, J., BERGER, R., LARSEN, C. AND TSAPIS, A.
The BCMA gene, preferentially expressed during B lymphoid maturation, is
bidirectionally transcribed.
NUCLEIC ACIDS RES. 22 1147-1154 (1994).
|
Documentation | 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 [1]. The
cysteines allow formation of an extended rod-like structure, responsible for
ligand binding [2].
Upon receptor activation, different intracellular signalling complexes are
assembled for different members of the TNFR superfamily, depending on their
intracellular domains and sequences [3]. 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 [4,5].
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 [3]. 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 [6].
TNF receptor 17 acts as a receptor for both a proliferation-inducing ligand
(APRIL) and B cell-activating factor (BAFF) [7]. It is preferentially
expressed by mature B-cells, suggesting a potential role for the receptor in
the B-cell developmental process [8].
TNFACTORR17 is a 3-element fingerprint that provides a signature for tumour
necrosis factor receptor 17. The fingerprint was derived from an initial
alignment of 2 sequences: the motifs were drawn from conserved regions in
the N-terminal three quarters of the alignment, focusing on those sections
that characterise TNF receptor 17 but distinguish it from other TNF receptor
subtypes - motif 1 lies in the extracellular N-terminal region; motif 2
resides partially in the transmembrane domain and partially in the
intracellular C-terminal region; and motif 3 lies wholly within the
intracellular C-terminal region. Two iterations on SPTR57_40f were required
to reach convergence, at which point a true set comprising 3 sequences was
identified. A single partial match was also also found, Q2TQ40_HUMAN, a
human splice variant that fails to match motif 2.
|