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基本情報
登録情報 | データベース: PDB / ID: 8zuk | ||||||||||||||||||||||||
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タイトル | Cluster structure of the BAFF-BAFFR-TRAF3 complex | ||||||||||||||||||||||||
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![]() | IMMUNE SYSTEM / Receptor cluster / Signal complex / membrane receptor | ||||||||||||||||||||||||
機能・相同性 | ![]() B cell costimulation / regulation of interferon-beta production / TRAF3 deficiency - HSE / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / Toll signaling pathway / CD40 receptor complex / regulation of defense response to virus / TRIF-dependent toll-like receptor signaling pathway / serine/threonine protein kinase complex / thioesterase binding ...B cell costimulation / regulation of interferon-beta production / TRAF3 deficiency - HSE / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / Toll signaling pathway / CD40 receptor complex / regulation of defense response to virus / TRIF-dependent toll-like receptor signaling pathway / serine/threonine protein kinase complex / thioesterase binding / tumor necrosis factor receptor binding / regulation of canonical NF-kappaB signal transduction / toll-like receptor 4 signaling pathway / toll-like receptor signaling pathway / negative regulation of NF-kappaB transcription factor activity / type I interferon-mediated signaling pathway / regulation of proteolysis / positive regulation of type I interferon production / ubiquitin ligase complex / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / TICAM1-dependent activation of IRF3/IRF7 / T cell costimulation / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / positive regulation of B cell proliferation / signaling adaptor activity / positive regulation of T cell proliferation / regulation of cytokine production / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / tumor necrosis factor-mediated signaling pathway / RING-type E3 ubiquitin transferase / SARS-CoV-1 activates/modulates innate immune responses / cytoplasmic side of plasma membrane / Ovarian tumor domain proteases / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / signaling receptor activity / TRAF3-dependent IRF activation pathway / protein phosphatase binding / regulation of apoptotic process / defense response to virus / adaptive immune response / cell surface receptor signaling pathway / endosome membrane / endosome / external side of plasma membrane / ubiquitin protein ligase binding / apoptotic process / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / signal transduction / mitochondrion / zinc ion binding / identical protein binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||||||||||||||||||||
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手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.83 Å | ||||||||||||||||||||||||
![]() | Lim, C.S. / Lee, J.O. | ||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Highly ordered clustering of TNFα and BAFF ligand-receptor-intracellular adaptor complexes on a lipid membrane. 著者: Chan Seok Lim / Jisun Lee / Ji Won Kim / Jie-Oh Lee / ![]() 要旨: The TNF family plays a critical role in immune regulation. Here, we present high-resolution structures of clusters formed by two TNF receptor family proteins, TNFR1 and BAFFR. Using a lipid monolayer ...The TNF family plays a critical role in immune regulation. Here, we present high-resolution structures of clusters formed by two TNF receptor family proteins, TNFR1 and BAFFR. Using a lipid monolayer method to mimic their membrane-bound state, we observe that the TNFα-TNFR1 complex forms highly ordered clusters of trimers on the lipid membrane. A non-competitive TNFR1 antagonist that inhibits receptor activation disrupted these clusters without blocking ligand binding or receptor trimerization. Furthermore, we find that the BAFF-BAFFR, BAFF-TACI, and BAFF-BCMA receptor-ligand complexes predominantly form pentagonal clusters of trimers on the lipid membrane. Notably, the binding of the intracellular adaptor TRAF3 to the BAFF-BAFFR complex induces a structural transition from a pentagonal to a flat hexagonal cluster. Mutations in BAFF that impair BAFFR activation prevented cluster formation. Our findings demonstrate that ligand binding induces the formation of highly ordered clusters of TNFR1 and BAFFR receptors on the lipid membrane, which is essential for their activation. | ||||||||||||||||||||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 935.9 KB | 表示 | ![]() |
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PDB形式 | ![]() | 673.1 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 1.7 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.7 MB | 表示 | |
XML形式データ | ![]() | 124.9 KB | 表示 | |
CIF形式データ | ![]() | 172.9 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 60486MC ![]() 8zuiC ![]() 8zujC C: 同じ文献を引用 ( M: このデータのモデリングに利用したマップデータ |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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リンク
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集合体
登録構造単位 | ![]()
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要素
#1: タンパク質 | 分子量: 35444.441 Da / 分子数: 21 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #2: タンパク質 | 分子量: 19902.789 Da / 分子数: 21 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() Has protein modification | N | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 | 名称: Cluster structure of the BAFF-BAFFR-TRAF3 complex / タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT | |||||||||||||||
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分子量 | 実験値: NO | |||||||||||||||
由来(天然) | 生物種: ![]() | |||||||||||||||
由来(組換発現) | 生物種: ![]() | |||||||||||||||
緩衝液 | pH: 7.8 | |||||||||||||||
緩衝液成分 |
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試料 | 濃度: 0.1 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | |||||||||||||||
試料支持 | グリッドの材料: GOLD / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 | |||||||||||||||
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 293 K |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: TFS KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 130000 X / 最大 デフォーカス(公称値): 2000 nm / 最小 デフォーカス(公称値): 800 nm |
撮影 | 電子線照射量: 40 e/Å2 フィルム・検出器のモデル: FEI FALCON IV (4k x 4k) |
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解析
EMソフトウェア | 名称: PHENIX / カテゴリ: モデル精密化 | |||||||||||||||||||||
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||
対称性 | 点対称性: C3 (3回回転対称) | |||||||||||||||||||||
3次元再構成 | 解像度: 2.83 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 205165 / 対称性のタイプ: POINT | |||||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT | |||||||||||||||||||||
原子モデル構築 |
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精密化 | 交差検証法: NONE |