1QSC

CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR

Summary for 1QSC

• Entry DOI: 10.2210/pdb1qsc/pdb
• Descriptor: TNF RECEPTOR ASSOCIATED FACTOR 2, CD40 RECEPTOR (3 entities in total)
• Functional Keywords: tnf signaling, traf, cd40 receptor, adapter protein, cell survival, coiled coil, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q12933
• Total number of polymer chains: 6
• Total formula weight: 68088.01

Authors

McWhirter, S.M.,Pullen, S.S.,Holton, J.M.,Crute, J.J.,Kehry, M.R.,Alber, T. (deposition date: 1999-06-20, release date: 1999-08-01, Last modification date: 2024-10-30)

Primary citation

McWhirter, S.M.,Pullen, S.S.,Holton, J.M.,Crute, J.J.,Kehry, M.R.,Alber, T.
Crystallographic analysis of CD40 recognition and signaling by human TRAF2.
Proc.Natl.Acad.Sci.USA, 96:8408-8413, 1999

PubMed Abstract: Tumor necrosis factor receptor superfamily members convey signals that promote diverse cellular responses. Receptor trimerization by extracellular ligands initiates signaling by recruiting members of the tumor necrosis factor receptor-associated factor (TRAF) family of adapter proteins to the receptor cytoplasmic domains. We report the 2.4-A crystal structure of a 22-kDa, receptor-binding fragment of TRAF2 complexed with a functionally defined peptide from the cytoplasmic domain of the CD40 receptor. TRAF2 forms a mushroom-shaped trimer consisting of a coiled coil and a unique beta-sandwich domain. Both domains mediate trimerization. The CD40 peptide binds in an extended conformation with every side chain in contact with a complementary groove on the rim of each TRAF monomer. The spacing between the CD40 binding sites on TRAF2 supports an elegant signaling mechanism in which trimeric, extracellular ligands preorganize the receptors to simultaneously recognize three sites on the TRAF trimer.

PubMed: 10411888
DOI: 10.1073/pnas.96.15.8408

Experimental method

X-RAY DIFFRACTION (2.4 Å)