1QSC

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

1QSC の概要

• エントリーDOI: 10.2210/pdb1qsc/pdb
• 分子名称: TNF RECEPTOR ASSOCIATED FACTOR 2, CD40 RECEPTOR (3 entities in total)
• 機能のキーワード: tnf signaling, traf, cd40 receptor, adapter protein, cell survival, coiled coil, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q12933
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 68088.01

構造登録者

McWhirter, S.M.,Pullen, S.S.,Holton, J.M.,Crute, J.J.,Kehry, M.R.,Alber, T. (登録日: 1999-06-20, 公開日: 1999-08-01, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)