Publication Date:
2000-07-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, F K -- Chun, H J -- Zheng, L -- Siegel, R M -- Bui, K L -- Lenardo, M J -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2351-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875917" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Substitution
;
Antigens, CD/chemistry/metabolism
;
Apoptosis
;
Binding Sites
;
Cross-Linking Reagents
;
Dimerization
;
Energy Transfer
;
Fluorescence
;
Humans
;
Ligands
;
Macromolecular Substances
;
Mutation
;
Protein Conformation
;
Protein Structure, Tertiary
;
Receptors, Tumor Necrosis Factor/*chemistry/*metabolism
;
Receptors, Tumor Necrosis Factor, Type I
;
Receptors, Tumor Necrosis Factor, Type II
;
Recombinant Fusion Proteins/chemistry/metabolism
;
*Signal Transduction
;
Succinimides
;
Tumor Cells, Cultured
;
Tumor Necrosis Factor-alpha/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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