1FLL

MOLECULAR BASIS FOR CD40 SIGNALING MEDIATED BY TRAF3

1FLL の概要

• エントリーDOI: 10.2210/pdb1fll/pdb
• 関連するPDBエントリー: 1FLK
• 分子名称: TNF RECEPTOR ASSOCIATED FACTOR 3, B-CELL SURFACE ANTIGEN CD40 (2 entities in total)
• 機能のキーワード: traf3 with cd40 peptide, tnf signaling, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (Probable): Q13114; Isoform I: Cell membrane; Single-pass type I membrane protein. Isoform II: Secreted: P25942
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56161.72

構造登録者

Ni, C.-Z.,Welsh, K.,Leo, E.,Chiou, C.-K.,Wu, H.,Reed, J.C.,Ely, K.R. (登録日: 2000-08-14, 公開日: 2000-10-18, 最終更新日: 2024-02-07)

主引用文献

Ni, C.Z.,Welsh, K.,Leo, E.,Chiou, C.K.,Wu, H.,Reed, J.C.,Ely, K.R.
Molecular basis for CD40 signaling mediated by TRAF3.
Proc.Natl.Acad.Sci.USA, 97:10395-10399, 2000

PubMed Abstract: Tumor necrosis factor receptors (TNFR) are single transmembrane-spanning glycoproteins that bind cytokines and trigger multiple signal transduction pathways. Many of these TNFRs rely on interactions with TRAF proteins that bind to the intracellular domain of the receptors. CD40 is a member of the TNFR family that binds to several different TRAF proteins. We have determined the crystal structure of a 20-residue fragment from the cytoplasmic domain of CD40 in complex with the TRAF domain of TRAF3. The CD40 fragment binds as a hairpin loop across the surface of the TRAF domain. Residues shown by mutagenesis and deletion analysis to be critical for TRAF3 binding are involved either in direct contact with TRAF3 or in intramolecular interactions that stabilize the hairpin. Comparison of the interactions of CD40 with TRAF3 vs. TRAF2 suggests that CD40 may assume different conformations when bound to different TRAF family members. This molecular adaptation may influence binding affinity and specific cellular triggers.

PubMed: 10984535
DOI: 10.1073/pnas.97.19.10395

実験手法

X-RAY DIFFRACTION (3.5 Å)