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3QO4

The Crystal Structure of Death Receptor 6

3QO4 の概要
エントリーDOI10.2210/pdb3qo4/pdb
分子名称Tumor necrosis factor receptor superfamily member 21, ACETATE ION, SULFATE ION, ... (4 entities in total)
機能のキーワードtumor necrosis factor receptor (tnfr), apoptosis, alzheimer s disease, ligand-receptor-recognition
由来する生物種Homo sapiens (human)
細胞内の位置Membrane; Single-pass type I membrane protein (Probable): O75509
タンパク質・核酸の鎖数1
化学式量合計19803.55
構造登録者
Kuester, M.,Kemmerzehl, S.,Dahms, S.O.,Roeser, D.,Than, M.E. (登録日: 2011-02-09, 公開日: 2011-05-18, 最終更新日: 2024-10-16)
主引用文献Kuester, M.,Kemmerzehl, S.,Dahms, S.O.,Roeser, D.,Than, M.E.
The crystal structure of death receptor 6 (DR6): a potential receptor of the amyloid precursor protein (APP).
J.Mol.Biol., 409:189-201, 2011
Cited by
PubMed Abstract: Death receptors belong to the tumor necrosis factor receptor (TNFR) super family and are intimately involved in the signal transduction during apoptosis, stress response and cellular survival. Here we present the crystal structure of recombinantly expressed death receptor six (DR6), one family member that was recently shown to bind to the amyloid precursor protein (APP) and hence to be probably involved in the development of Alzheimer's disease. The extracellular cysteine rich region of DR6, the typical ligand binding region of all TNFRs, was refined to 2.2 Å resolution and shows that its four constituting cysteine rich domains (CRDs) are arranged in a rod-like overall structure, which presents DR6-specific surface patches responsible for the exclusive recognition of its ligand(s). Based on the structural data, the general ligand binding modes of TNFRs and molecular modeling experiments we were able to elucidate structural features of the potential DR6-APP signaling complex.
PubMed: 21463639
DOI: 10.1016/j.jmb.2011.03.048
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 3qo4
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2026-04-22に公開中

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