+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-36124 | |||||||||||||||
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タイトル | Structure of beta-arrestin1 in complex with C3aRpp | |||||||||||||||
マップデータ | ||||||||||||||||
試料 |
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キーワード | GPCR / Arrestin / SIGNALING PROTEIN / SIGNALING PROTEIN-IMMUNE SYSTEM complex | |||||||||||||||
機能・相同性 | 機能・相同性情報 V2 vasopressin receptor binding / complement component C3a receptor activity / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / TGFBR3 regulates TGF-beta signaling / sensory perception of touch / G alpha (s) signalling events / alpha-1B adrenergic receptor binding / complement component C5a receptor activity / follicle-stimulating hormone signaling pathway ...V2 vasopressin receptor binding / complement component C3a receptor activity / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / TGFBR3 regulates TGF-beta signaling / sensory perception of touch / G alpha (s) signalling events / alpha-1B adrenergic receptor binding / complement component C5a receptor activity / follicle-stimulating hormone signaling pathway / protein phosphorylated amino acid binding / angiotensin receptor binding / Lysosome Vesicle Biogenesis / AP-2 adaptor complex binding / Golgi Associated Vesicle Biogenesis / MAP2K and MAPK activation / Ub-specific processing proteases / positive regulation of smooth muscle cell apoptotic process / negative regulation of interleukin-8 production / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / clathrin adaptor activity / complement receptor mediated signaling pathway / regulation of G protein-coupled receptor signaling pathway / arrestin family protein binding / G protein-coupled receptor internalization / positive regulation of neutrophil chemotaxis / blood circulation / Thrombin signalling through proteinase activated receptors (PARs) / response to morphine / mitogen-activated protein kinase kinase binding / azurophil granule membrane / positive regulation of Rho protein signal transduction / clathrin binding / positive regulation of macrophage chemotaxis / stress fiber assembly / negative regulation of Notch signaling pathway / positive regulation of receptor internalization / pseudopodium / positive regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of interleukin-6 production / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / phototransduction / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / specific granule membrane / clathrin-coated pit / negative regulation of protein ubiquitination / insulin-like growth factor receptor binding / visual perception / GTPase activator activity / negative regulation of protein phosphorylation / Peptide ligand-binding receptors / positive regulation of protein ubiquitination / Regulation of Complement cascade / nuclear estrogen receptor binding / G protein-coupled receptor binding / G protein-coupled receptor activity / phosphoprotein binding / calcium-mediated signaling / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / negative regulation of ERK1 and ERK2 cascade / endocytosis / positive regulation of angiogenesis / chemotaxis / protein transport / positive regulation of peptidyl-serine phosphorylation / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / G alpha (i) signalling events / ubiquitin-dependent protein catabolic process / cytoplasmic vesicle / basolateral plasma membrane / regulation of apoptotic process / postsynaptic membrane / proteasome-mediated ubiquitin-dependent protein catabolic process / negative regulation of neuron apoptotic process / transmembrane transporter binding / positive regulation of MAPK cascade / dendritic spine / transcription coactivator activity / positive regulation of ERK1 and ERK2 cascade / postsynaptic density / endosome / protein ubiquitination / inflammatory response / response to xenobiotic stimulus / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / signaling receptor binding / glutamatergic synapse / positive regulation of cell population proliferation / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of DNA-templated transcription / chromatin / negative regulation of apoptotic process / regulation of transcription by RNA polymerase II / enzyme binding / positive regulation of transcription by RNA polymerase II 類似検索 - 分子機能 | |||||||||||||||
生物種 | Rattus norvegicus (ドブネズミ) / Mus musculus (ハツカネズミ) / Homo sapiens (ヒト) | |||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.94 Å | |||||||||||||||
データ登録者 | Maharana J / Sarma P / Yadav MK / Chami M / Banerjee R / Shukla AK | |||||||||||||||
資金援助 | インド, 4件
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引用 | ジャーナル: Science / 年: 2024 タイトル: Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. 著者: Jagannath Maharana / Fumiya K Sano / Parishmita Sarma / Manish K Yadav / Longhan Duan / Tomasz M Stepniewski / Madhu Chaturvedi / Ashutosh Ranjan / Vinay Singh / Sayantan Saha / Gargi Mahajan ...著者: Jagannath Maharana / Fumiya K Sano / Parishmita Sarma / Manish K Yadav / Longhan Duan / Tomasz M Stepniewski / Madhu Chaturvedi / Ashutosh Ranjan / Vinay Singh / Sayantan Saha / Gargi Mahajan / Mohamed Chami / Wataru Shihoya / Jana Selent / Ka Young Chung / Ramanuj Banerjee / Osamu Nureki / Arun K Shukla / 要旨: β-arrestins (βarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor ...β-arrestins (βarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor activation and phosphorylation. Here, we present seven cryo-electron microscopy structures of βarrs either in the basal state, activated by the muscarinic receptor subtype 2 (M2R) through its third intracellular loop, or activated by the βarr-biased decoy D6 receptor (D6R). Combined with biochemical, cellular, and biophysical experiments, these structural snapshots allow the visualization of atypical engagement of βarrs with 7TMRs and also reveal a structural transition in the carboxyl terminus of βarr2 from a β strand to an α helix upon activation by D6R. Our study provides previously unanticipated molecular insights into the structural and functional diversity encoded in 7TMR-βarr complexes with direct implications for exploring novel therapeutic avenues. | |||||||||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_36124.map.gz | 56.7 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-36124-v30.xml emd-36124.xml | 22.6 KB 22.6 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_36124_fsc.xml | 8.4 KB | 表示 | FSCデータファイル |
画像 | emd_36124.png | 64 KB | ||
Filedesc metadata | emd-36124.cif.gz | 7 KB | ||
その他 | emd_36124_half_map_1.map.gz emd_36124_half_map_2.map.gz | 59.3 MB 59.3 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-36124 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36124 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_36124_validation.pdf.gz | 720.3 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_36124_full_validation.pdf.gz | 719.9 KB | 表示 | |
XML形式データ | emd_36124_validation.xml.gz | 16.1 KB | 表示 | |
CIF形式データ | emd_36124_validation.cif.gz | 21 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36124 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36124 | HTTPS FTP |
-関連構造データ
関連構造データ | 8ja3MC 8go9C 8j8rC 8j8vC 8j8zC 8j97C 8j9kC 8jafC M: このマップから作成された原子モデル 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
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_36124.map.gz / 形式: CCP4 / 大きさ: 64 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.4268 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-ハーフマップ: #2
ファイル | emd_36124_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_36124_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
-全体 : beta-arrestin1 in complex with C3aRpp
全体 | 名称: beta-arrestin1 in complex with C3aRpp |
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要素 |
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-超分子 #1: beta-arrestin1 in complex with C3aRpp
超分子 | 名称: beta-arrestin1 in complex with C3aRpp / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all |
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-超分子 #2: beta-arrestin-1
超分子 | 名称: beta-arrestin-1 / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #1 |
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由来(天然) | 生物種: Rattus norvegicus (ドブネズミ) |
-超分子 #3: Fab30 Heavy Chain
超分子 | 名称: Fab30 Heavy Chain / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #3 |
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由来(天然) | 生物種: Mus musculus (ハツカネズミ) |
-超分子 #4: Fab30 Light Chain
超分子 | 名称: Fab30 Light Chain / タイプ: complex / ID: 4 / 親要素: 1 / 含まれる分子: #4 |
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由来(天然) | 生物種: Mus musculus (ハツカネズミ) |
-超分子 #5: Phosphopeptide derived from the C-terminal tail of C3aR receptor ...
超分子 | 名称: Phosphopeptide derived from the C-terminal tail of C3aR receptor (C3aRpp) タイプ: complex / ID: 5 / 親要素: 1 / 含まれる分子: #2 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: Beta-arrestin-1
分子 | 名称: Beta-arrestin-1 / タイプ: protein_or_peptide / ID: 1 / コピー数: 2 / 光学異性体: LEVO |
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由来(天然) | 生物種: Rattus norvegicus (ドブネズミ) |
分子量 | 理論値: 40.075152 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA FRYGREDLDV LGLTFRKDLF VANVQSFPP APEDKKPLTR LQERLIKKLG EHAYPFTFEI PPNLPCSVTL QPGPEDTGKA CGVDYEVKAF CAENLEEKIH K RNSVRLVI ...文字列: MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA FRYGREDLDV LGLTFRKDLF VANVQSFPP APEDKKPLTR LQERLIKKLG EHAYPFTFEI PPNLPCSVTL QPGPEDTGKA CGVDYEVKAF CAENLEEKIH K RNSVRLVI RKVQYAPERP GPQPTAETTR QFLMSDKPLH LEASLDKEIY YHGEPISVNV HVTNNTNKTV KKIKISVRQY AD ICLFNTA QYKCPVAMEE ADDTVAPSST FCKVYTLTPF LANNREKRGL ALDGKLKHED TNLASSTLLR EGANREILGI IVS YKVKVK LVVSRGGLLG DLASSDVAVE LPFTLMHPKP K UniProtKB: Beta-arrestin-1 |
-分子 #2: C3a anaphylatoxin chemotactic receptor
分子 | 名称: C3a anaphylatoxin chemotactic receptor / タイプ: protein_or_peptide / ID: 2 / コピー数: 2 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 1.484165 KDa |
配列 | 文字列: (SEP)EEL(TPO)R(SEP)(TPO)HC UniProtKB: C3a anaphylatoxin chemotactic receptor |
-分子 #3: Fab30 heavy chain
分子 | 名称: Fab30 heavy chain / タイプ: protein_or_peptide / ID: 3 / コピー数: 2 / 光学異性体: LEVO |
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由来(天然) | 生物種: Mus musculus (ハツカネズミ) |
分子量 | 理論値: 25.512354 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: EISEVQLVES GGGLVQPGGS LRLSCAASGF NVYSSSIHWV RQAPGKGLEW VASISSYYGY TYYADSVKGR FTISADTSKN TAYLQMNSL RAEDTAVYYC ARSRQFWYSG LDYWGQGTLV TVSSASTKGP SVFPLAPSSK STSGGTAALG CLVKDYFPEP V TVSWNSGA ...文字列: EISEVQLVES GGGLVQPGGS LRLSCAASGF NVYSSSIHWV RQAPGKGLEW VASISSYYGY TYYADSVKGR FTISADTSKN TAYLQMNSL RAEDTAVYYC ARSRQFWYSG LDYWGQGTLV TVSSASTKGP SVFPLAPSSK STSGGTAALG CLVKDYFPEP V TVSWNSGA LTSGVHTFPA VLQSSGLYSL SSVVTVPSSS LGTQTYICNV NHKPSNTKVD KKVEPKSCDK THHHHHHHH |
-分子 #4: Fab30 light chain
分子 | 名称: Fab30 light chain / タイプ: protein_or_peptide / ID: 4 / コピー数: 2 / 光学異性体: LEVO |
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由来(天然) | 生物種: Mus musculus (ハツカネズミ) |
分子量 | 理論値: 23.435064 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQYKYVPVTF GQGTKVEIKR TVAAPSVFIF PPSDSQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD ...文字列: SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQYKYVPVTF GQGTKVEIKR TVAAPSVFIF PPSDSQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK SFNRGEC |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.4 構成要素:
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凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | TFS GLACIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 検出モード: COUNTING / 実像数: 13438 / 平均電子線量: 49.4 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 0.5 µm / 倍率(公称値): 46000 |
試料ステージ | ホルダー冷却材: NITROGEN |