Article
The pre-ligand binding assembly domain: a potential target of
inhibition of tumour necrosis factor receptor function
Francis Ka-Ming Chan
Building 10, Room
11N311, Laboratory of Immunology, National Institute of Allergy and
Infectious Diseases, National Institutes of Health, Bethesda, MD
20892-1892, USA
Correspondence to: Dr Chan (fchan{at}nih.gov)
Signalling by the tumour necrosis factor receptors (TNFR)
is thought to be mediated by the binding of the trimeric ligand TNF to
three monomeric subunits of the receptor. This ligand induced trimerisation model of TNFR signalling is mainly supported by crystallographic data of the p60 TNFR-1 and TNF
complex in which the
trimeric ligand interdigitates between the individual receptor chains
and prevents the receptor subunits from interacting with each other.
Recently, a domain NH2-terminal to the ligand binding domain in the extracellular region of p60 TNFR-1, p80 TNFR-2 and Fas
was identified that mediates receptor self association before ligand
binding. This pre-ligand binding assembly domain or PLAD is critical
for assembly of functional receptor complexes on the cell surface and
may provide a potential target in the design of future novel
therapeutics against diseases mediated by members of the TNFR family of receptors.
© 2000 by Annals of the Rheumatic Diseases
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