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3M0A

Crystal structure of TRAF2:cIAP2 complex

3M0A の概要
エントリーDOI10.2210/pdb3m0a/pdb
関連するPDBエントリー3M06 3M0D
分子名称TNF receptor-associated factor 2, Baculoviral IAP repeat-containing protein 3, ZINC ION, ... (4 entities in total)
機能のキーワードtraf2: ciap2 and the traf1: traf2: ciap2 complexes, apoptosis, metal-binding, phosphoprotein, signaling protein
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cytoplasm : Q12933 Q13489
タンパク質・核酸の鎖数4
化学式量合計31365.22
構造登録者
Kabaleeswaran, V.,Wu, H. (登録日: 2010-03-02, 公開日: 2010-04-28, 最終更新日: 2024-02-21)
主引用文献Zheng, C.,Kabaleeswaran, V.,Wang, Y.,Cheng, G.,Wu, H.
Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.
Mol.Cell, 38:101-113, 2010
Cited by
PubMed Abstract: TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by mutagenesis. TRAF1 and TRAF2 preferentially form the TRAF1: (TRAF2)(2) heterotrimer, which interacts with cIAP2 more strongly than TRAF2 alone. In contrast, TRAF1 alone interacts very weakly with cIAP2. Surprisingly, TRAF1 and one chain of TRAF2 in the TRAF1: (TRAF2)(2): cIAP2 ternary complex mediate interaction with cIAP2. Because TRAF1 is upregulated by many stimuli, it may modulate the interaction of TRAF2 with cIAP1/2, which explains regulatory roles of TRAF1 in TNF signaling.
PubMed: 20385093
DOI: 10.1016/j.molcel.2010.03.009
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.61 Å)
構造検証レポート
Validation report summary of 3m0a
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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