A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling.

Published

Journal Article

A conserved domain in the extracellular region of the 60- and 80-kilodalton tumor necrosis factor receptors (TNFRs) was identified that mediates specific ligand-independent assembly of receptor trimers. This pre-ligand-binding assembly domain (PLAD) is physically distinct from the domain that forms the major contacts with ligand, but is necessary and sufficient for the assembly of TNFR complexes that bind TNF-alpha and mediate signaling. Other members of the TNFR superfamily, including TRAIL receptor 1 and CD40, show similar homotypic association. Thus, TNFRs and related receptors appear to function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding.

Full Text

Duke Authors

Cited Authors

  • Chan, FK; Chun, HJ; Zheng, L; Siegel, RM; Bui, KL; Lenardo, MJ

Published Date

  • June 30, 2000

Published In

Volume / Issue

  • 288 / 5475

Start / End Page

  • 2351 - 2354

PubMed ID

  • 10875917

Pubmed Central ID

  • 10875917

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.288.5475.2351

Language

  • eng

Conference Location

  • United States