+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 8h77 | ||||||
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タイトル | Hsp90-AhR-p23-XAP2 complex | ||||||
要素 |
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キーワード | CYTOSOLIC PROTEIN / Hsp90 / AhR / PASB doamin / complex / p23 / XAP2 | ||||||
機能・相同性 | 機能・相同性情報 circumferential growth involved in left ventricle morphogenesis / negative regulation of calcium ion transmembrane transport / cellular response to 3-methylcholanthrene / regulation of heart growth / GAF domain binding / ESR-mediated signaling / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome ...circumferential growth involved in left ventricle morphogenesis / negative regulation of calcium ion transmembrane transport / cellular response to 3-methylcholanthrene / regulation of heart growth / GAF domain binding / ESR-mediated signaling / cytosolic aryl hydrocarbon receptor complex / glomerulus morphogenesis / DDX58/IFIH1-mediated induction of interferon-alpha/beta / The NLRP3 inflammasome / gland development / HSF1-dependent transactivation / reactive oxygen species biosynthetic process / Phase I - Functionalization of compounds / Xenobiotics / Aryl hydrocarbon receptor signalling / HSF1 activation / kidney morphogenesis / RHOBTB2 GTPase cycle / lung saccule development / ooplasm / Sema3A PAK dependent Axon repulsion / omega-hydroxylase P450 pathway / prostaglandin-E synthase / prostaglandin-E synthase activity / arachidonate omega-hydroxylase activity / positive regulation of growth rate / Attenuation phase / lymphocyte homeostasis / regulation of adaptive immune response / receptor ligand inhibitor activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / negative regulation of complement-dependent cytotoxicity / cellular response to 2,3,7,8-tetrachlorodibenzodioxine / telomerase activity / Endogenous sterols / nuclear aryl hydrocarbon receptor complex / HSP90-CDC37 chaperone complex / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / negative regulation of cyclic-nucleotide phosphodiesterase activity / nuclear receptor-mediated glucocorticoid signaling pathway / sperm head plasma membrane / cardiac left ventricle morphogenesis / The role of GTSE1 in G2/M progression after G2 checkpoint / negative regulation of proteasomal protein catabolic process / negative regulation of osteoblast proliferation / prostate gland development / reproductive structure development / cellular response to toxic substance / aryl hydrocarbon receptor complex / negative regulation of T cell mediated immune response to tumor cell / Regulation of actin dynamics for phagocytic cup formation / dynein axonemal particle / histone methyltransferase binding / B-1 B cell homeostasis / Estrogen-dependent gene expression / regulation of protein kinase A signaling / COP9 signalosome / post-embryonic hemopoiesis / E-box binding / negative regulation of DNA biosynthetic process / protein targeting to mitochondrion / positive regulation of protein localization to cell surface / ATP-dependent protein binding / vasculature development / camera-type eye development / negative regulation of systemic arterial blood pressure / telomerase holoenzyme complex / blood circulation / glycogen biosynthetic process / protein folding chaperone complex / negative regulation of protein metabolic process / blood vessel morphogenesis / prostaglandin biosynthetic process / protein maturation by protein folding / dATP binding / sulfonylurea receptor binding / CTP binding / UTP binding / skin development / negative regulation of vasoconstriction / telomerase holoenzyme complex assembly / branching involved in blood vessel morphogenesis / immune system process / prostaglandin metabolic process / negative regulation of osteoblast differentiation / heterocyclic compound binding / TPR domain binding / blood vessel development / positive regulation of transforming growth factor beta receptor signaling pathway / T cell homeostasis / dendritic growth cone / positive regulation of phosphorylation / aryl hydrocarbon receptor binding / B cell homeostasis / : / regulation of protein ubiquitination / chaperone cofactor-dependent protein refolding / telomere maintenance via telomerase / positive regulation of cell size 類似検索 - 分子機能 | ||||||
生物種 | Mus musculus (ハツカネズミ) | ||||||
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: 3.2 Å | ||||||
データ登録者 | Wen, Z.L. / Zhai, Y.J. / Zhu, Y. / Sun, F. | ||||||
資金援助 | 1件
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引用 | ジャーナル: Structure / 年: 2023 タイトル: Cryo-EM structure of the cytosolic AhR complex. 著者: Zuoling Wen / Yuebin Zhang / Beirong Zhang / Yumo Hang / Li Xu / Yangsheng Chen / Qunhui Xie / Qun Zhao / Lihua Zhang / Guohui Li / Bin Zhao / Fei Sun / Yujia Zhai / Yun Zhu / 要旨: Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures ...Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures of the Hsp90-AhR-p23 complex with or without bound XAP2, where the structure of the mouse AhR PAS-B domain is resolved. A highly conserved bridge motif of AhR is responsible for the interaction with the Hsp90 dimeric lumen. The ligand-free AhR PAS-B domain is attached to the Hsp90 dimer and is stabilized in the complex with bound XAP2. In addition, the DE-loop and a group of conserved pocket inner residues in the AhR PAS-B domain are found to be important for ligand binding. These results reveal the structural basis of the biological functions of AhR. Moreover, the protein purification method presented here allows the isolation of stable mouse AhR protein, which could be used to develop high-sensitivity biosensors for environmental pollutant detection. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 8h77.cif.gz | 366.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb8h77.ent.gz | 286.4 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 8h77.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/h7/8h77 ftp://data.pdbj.org/pub/pdb/validation_reports/h7/8h77 | HTTPS FTP |
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-関連構造データ
関連構造データ | 34519MC 7y04C M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
-タンパク質 , 4種, 6分子 ABCDEF
#1: タンパク質 | 分子量: 86590.688 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 遺伝子: Hsp90ab1, Hsp84, Hsp84-1, Hspcb 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: P11499 #2: タンパク質 | 分子量: 20133.994 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 遺伝子: Ptges3, Sid3177, Tebp 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: Q9R0Q7, prostaglandin-E synthase #3: タンパク質 | | 分子量: 50507.441 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 遺伝子: Ahr 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: P30561 #4: タンパク質 | | 分子量: 38744.102 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 遺伝子: Aip 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: O08915 |
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-非ポリマー , 2種, 4分子
#5: 化合物 | #6: 化合物 | |
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-詳細
研究の焦点であるリガンドがあるか | 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 |
-試料調製
構成要素 |
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由来(天然) |
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由来(組換発現) |
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緩衝液 | pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
-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: FEI TITAN KRIOS |
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 1800 nm / 最小 デフォーカス(公称値): 1200 nm |
撮影 | 電子線照射量: 60 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.18.2_3874: / 分類: 精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 266830 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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