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A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling

Science  30 Jun 2000:
Vol. 288, Issue 5475, pp. 2351-2354
DOI: 10.1126/science.288.5475.2351

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Abstract

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-α 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.

  • * Present address: George Washington University School of Medicine, Washington, DC 20037, USA.

  • To whom correspondence should be addressed. E-mail: Lenardo{at}nih.gov

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