1rf3
From Proteopedia
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, resolution 3.5Å | |||||||
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Gene: | TRAF3 OR CRAF1 OR CAP1 (Homo sapiens) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structurally Distinct Recognition Motifs in Lymphotoxin-B Receptor and CD40 for TRAF-mediated Signaling
Overview
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 Structure
1RF3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 23:27:14 2008
Categories: Homo sapiens | Protein complex | Cabezas, E. | Cheng, G. | Chiong, E M. | Ely, K R. | Havert, M L. | Li, C. | Ni, C Z. | Norris, P S. | Reed, J C. | Satterthwait, A C. | Tran, B R. | Ware, C F. | Cd40 | Ltbr | Nf-kb signaling | Tnf receptor | Traf3 crystallography