+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6up7 | ||||||
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タイトル | neurotensin receptor and arrestin2 complex | ||||||
要素 |
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キーワード | MEMBRANE PROTEIN / GPCR signaling | ||||||
機能・相同性 | 機能・相同性情報 neuropeptide receptor binding / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / angiotensin receptor binding / symmetric synapse / D-aspartate import across plasma membrane / TGFBR3 regulates TGF-beta signaling / Activation of SMO / positive regulation of gamma-aminobutyric acid secretion / positive regulation of inhibitory postsynaptic potential ...neuropeptide receptor binding / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / angiotensin receptor binding / symmetric synapse / D-aspartate import across plasma membrane / TGFBR3 regulates TGF-beta signaling / Activation of SMO / positive regulation of gamma-aminobutyric acid secretion / positive regulation of inhibitory postsynaptic potential / negative regulation of interleukin-8 production / regulation of membrane depolarization / positive regulation of arachidonate secretion / L-glutamate import across plasma membrane / regulation of respiratory gaseous exchange / neuropeptide hormone activity / positive regulation of glutamate secretion / arrestin family protein binding / G protein-coupled receptor internalization / negative regulation of systemic arterial blood pressure / negative regulation of release of sequestered calcium ion into cytosol / enzyme inhibitor activity / Lysosome Vesicle Biogenesis / positive regulation of inositol phosphate biosynthetic process / negative regulation of NF-kappaB transcription factor activity / positive regulation of Rho protein signal transduction / Golgi Associated Vesicle Biogenesis / temperature homeostasis / response to lipid / stress fiber assembly / negative regulation of Notch signaling pathway / positive regulation of receptor internalization / pseudopodium / detection of temperature stimulus involved in sensory perception of pain / negative regulation of interleukin-6 production / neuropeptide signaling pathway / clathrin-coated pit / axon terminus / negative regulation of protein ubiquitination / transport vesicle / insulin-like growth factor receptor binding / visual perception / GTPase activator activity / Activated NOTCH1 Transmits Signal to the Nucleus / blood vessel diameter maintenance / Peptide ligand-binding receptors / adult locomotory behavior / positive regulation of release of sequestered calcium ion into cytosol / learning / dendritic shaft / G protein-coupled receptor binding / G protein-coupled receptor activity / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / cytoplasmic vesicle membrane / terminal bouton / cytoplasmic side of plasma membrane / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / protein transport / Cargo recognition for clathrin-mediated endocytosis / Thrombin signalling through proteinase activated receptors (PARs) / Clathrin-mediated endocytosis / positive regulation of NF-kappaB transcription factor activity / ubiquitin-dependent protein catabolic process / cytoplasmic vesicle / G alpha (s) signalling events / chemical synaptic transmission / G alpha (q) signalling events / perikaryon / proteasome-mediated ubiquitin-dependent protein catabolic process / dendritic spine / transcription coactivator activity / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / nuclear body / Ub-specific processing proteases / receptor ligand activity / protein ubiquitination / positive regulation of apoptotic process / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / membrane raft / lysosomal membrane / Golgi membrane / negative regulation of gene expression / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / protein-containing complex binding / positive regulation of gene expression / chromatin / negative regulation of apoptotic process / regulation of transcription by RNA polymerase II / Golgi apparatus / cell surface / endoplasmic reticulum / signal transduction 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
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: 4.2 Å | ||||||
データ登録者 | Qu, Q.H. / Huang, W. / Masureel, M. / Janetzko, J. / Kobilka, B.K. / Skiniotis, G. | ||||||
引用 | ジャーナル: Nature / 年: 2020 タイトル: Structure of the neurotensin receptor 1 in complex with β-arrestin 1. 著者: Weijiao Huang / Matthieu Masureel / Qianhui Qu / John Janetzko / Asuka Inoue / Hideaki E Kato / Michael J Robertson / Khanh C Nguyen / Jeffrey S Glenn / Georgios Skiniotis / Brian K Kobilka / 要旨: Arrestin proteins bind to active, phosphorylated G-protein-coupled receptors (GPCRs), thereby preventing G-protein coupling, triggering receptor internalization and affecting various downstream ...Arrestin proteins bind to active, phosphorylated G-protein-coupled receptors (GPCRs), thereby preventing G-protein coupling, triggering receptor internalization and affecting various downstream signalling pathways. Although there is a wealth of structural information detailing the interactions between GPCRs and G proteins, less is known about how arrestins engage GPCRs. Here we report a cryo-electron microscopy structure of full-length human neurotensin receptor 1 (NTSR1) in complex with truncated human β-arrestin 1 (βarr1(ΔCT)). We find that phosphorylation of NTSR1 is critical for the formation of a stable complex with βarr1(ΔCT), and identify phosphorylated sites in both the third intracellular loop and the C terminus that may promote this interaction. In addition, we observe a phosphatidylinositol-4,5-bisphosphate molecule forming a bridge between the membrane side of NTSR1 transmembrane segments 1 and 4 and the C-lobe of arrestin. Compared with a structure of a rhodopsin-arrestin-1 complex, in our structure arrestin is rotated by approximately 85° relative to the receptor. These findings highlight both conserved aspects and plasticity among arrestin-receptor interactions. | ||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 6up7.cif.gz | 128.4 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6up7.ent.gz | 94.3 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 6up7.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
文書・要旨 | 6up7_validation.pdf.gz | 730.7 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6up7_full_validation.pdf.gz | 736.6 KB | 表示 | |
XML形式データ | 6up7_validation.xml.gz | 24.3 KB | 表示 | |
CIF形式データ | 6up7_validation.cif.gz | 36.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/up/6up7 ftp://data.pdbj.org/pub/pdb/validation_reports/up/6up7 | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
#1: タンパク質・ペプチド | 分子量: 819.007 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: P30990*PLUS |
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#2: タンパク質 | 分子量: 39062.840 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ARRB1, ARR1 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: P49407 |
#3: タンパク質 | 分子量: 37360.656 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: missing regions were not modeled due to local low resolution/flexibility. 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: NTSR1, NTRR 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 参照: UniProt: P30989 |
#4: タンパク質・ペプチド | 分子量: 783.958 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: actual sequence for this poly-A exists, however, the local resolution for this region is not sufficient to register the amino acids. 由来: (組換発現) Homo sapiens (ヒト) 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) |
#5: 化合物 | ChemComp-PIO / [( |
研究の焦点であるリガンドがあるか | Y |
-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 | 名称: NTSR_Arrestin / タイプ: COMPLEX / Entity ID: #1-#4 / 由来: RECOMBINANT |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
由来(組換発現) | 生物種: Spodoptera frugiperda (ツマジロクサヨトウ) |
緩衝液 | pH: 7.4 |
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: OTHER |
撮影 | 電子線照射量: 56 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
-解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 254725 / 対称性のタイプ: POINT |