The pre-ligand binding assembly domain: a potential target of inhibition of tumour necrosis factor receptor function.

Published

Journal Article (Review)

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 TNFbeta 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 NH(2)-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.

Full Text

Duke Authors

Cited Authors

  • Chan, FK

Published Date

  • November 2000

Published In

Volume / Issue

  • 59 Suppl 1 /

Start / End Page

  • i50 - i53

PubMed ID

  • 11053089

Pubmed Central ID

  • 11053089

Electronic International Standard Serial Number (EISSN)

  • 1468-2060

International Standard Serial Number (ISSN)

  • 0003-4967

Digital Object Identifier (DOI)

  • 10.1136/ard.59.suppl_1.i50

Language

  • eng