1rf3
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Structurally Distinct Recognition Motifs in Lymphotoxin-B Receptor and CD40 for TRAF-mediated Signaling
OverviewOverview
Lymphotoxin-beta receptor (LTbetaR) and CD40 are members of the tumor, necrosis factor family of signaling receptors that regulate cell survival, or death through activation of NF-kappaB. These receptors transmit signals, through downstream adaptor proteins called tumor necrosis factor, receptor-associated factors (TRAFs). In this study, the crystal structure, of a region of the cytoplasmic domain of LTbetaR bound to TRAF3 has, revealed an unexpected new recognition motif, 388IPEEGD393, for TRAF3, binding. Although this motif is distinct in sequence and structure from, the PVQET motif in CD40 and PIQCT in the regulator TRAF-associated, NF-kappaB activator (TANK), recognition is mediated in the same binding, crevice on the surface of TRAF3. The results reveal structurally adaptive, "hot spots" in the TRAF3-binding crevice that promote molecular, interactions driving specific signaling after contact with LTbetaR, CD40, or the downstream regulator TANK.
About this StructureAbout this Structure
1RF3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structurally distinct recognition motifs in lymphotoxin-beta receptor and CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated signaling., Li C, Norris PS, Ni CZ, Havert ML, Chiong EM, Tran BR, Cabezas E, Reed JC, Satterthwait AC, Ware CF, Ely KR, J Biol Chem. 2003 Dec 12;278(50):50523-9. Epub 2003 Sep 29. PMID:14517219
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