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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 8gp3 | ||||||
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タイトル | Structure of beta-arrestin1 in complex with a phosphopeptide corresponding to the human C-X-C chemokine receptor type 4, CXCR4 | ||||||
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![]() | SIGNALING PROTEIN / GPCR / Arrestin | ||||||
機能・相同性 | ![]() V2 vasopressin receptor binding / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / sensory perception of touch / C-X-C motif chemokine 12 receptor activity / G alpha (s) signalling events / regulation of viral process / alpha-1B adrenergic receptor binding / positive regulation of vascular wound healing / follicle-stimulating hormone signaling pathway ...V2 vasopressin receptor binding / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / sensory perception of touch / C-X-C motif chemokine 12 receptor activity / G alpha (s) signalling events / regulation of viral process / alpha-1B adrenergic receptor binding / positive regulation of vascular wound healing / follicle-stimulating hormone signaling pathway / protein phosphorylated amino acid binding / positive regulation of macrophage migration inhibitory factor signaling pathway / angiotensin receptor binding / positive regulation of mesenchymal stem cell migration / neuron recognition / response to ultrasound / response to tacrolimus / telencephalon cell migration / C-X-C chemokine receptor activity / Specification of primordial germ cells / CXCL12-activated CXCR4 signaling pathway / Lysosome Vesicle Biogenesis / myosin light chain binding / AP-2 adaptor complex binding / Golgi Associated Vesicle Biogenesis / MAP2K and MAPK activation / Ub-specific processing proteases / myelin maintenance / positive regulation of vasculature development / regulation of programmed cell death / positive regulation of smooth muscle cell apoptotic process / endothelial tube morphogenesis / endothelial cell differentiation / negative regulation of interleukin-8 production / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / clathrin adaptor activity / Signaling by ROBO receptors / regulation of chemotaxis / : / positive regulation of dendrite extension / Formation of definitive endoderm / positive regulation of chemotaxis / C-C chemokine receptor activity / regulation of G protein-coupled receptor signaling pathway / C-C chemokine binding / arrestin family protein binding / G protein-coupled receptor internalization / response to morphine / Chemokine receptors bind chemokines / Thrombin signalling through proteinase activated receptors (PARs) / anchoring junction / dendritic cell chemotaxis / mitogen-activated protein kinase kinase binding / clathrin binding / positive regulation of oligodendrocyte differentiation / positive regulation of Rho protein signal transduction / stress fiber assembly / negative regulation of Notch signaling pathway / cell leading edge / epithelial cell development / pseudopodium / cellular response to cytokine stimulus / positive regulation of insulin secretion involved in cellular response to glucose stimulus / detection of temperature stimulus involved in sensory perception of pain / regulation of calcium ion transport / negative regulation of interleukin-6 production / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / positive regulation of receptor internalization / phototransduction / small molecule binding / Binding and entry of HIV virion / regulation of cell adhesion / coreceptor activity / detection of mechanical stimulus involved in sensory perception of pain / cardiac muscle contraction / clathrin-coated pit / negative regulation of protein ubiquitination / visual perception / GTPase activator activity / neurogenesis / cell chemotaxis / negative regulation of protein phosphorylation / ubiquitin binding / response to activity / positive regulation of protein ubiquitination / G protein-coupled receptor binding / G protein-coupled receptor activity / nuclear estrogen receptor binding / calcium-mediated signaling / phosphoprotein binding / insulin-like growth factor receptor binding / neuron migration / response to virus / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / brain development / negative regulation of ERK1 and ERK2 cascade / endocytosis / protein transport / cellular response to xenobiotic stimulus 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() ![]() ![]() | ||||||
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: 4.8 Å | ||||||
![]() | Maharana, J. / Sarma, P. / Yadav, M.K. / Banerjee, R. / Shukla, A.K. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation. 著者: Jagannath Maharana / Parishmita Sarma / Manish K Yadav / Sayantan Saha / Vinay Singh / Shirsha Saha / Mohamed Chami / Ramanuj Banerjee / Arun K Shukla / ![]() ![]() 要旨: Agonist-induced GPCR phosphorylation is a key determinant for the binding and activation of β-arrestins (βarrs). However, it is not entirely clear how different GPCRs harboring divergent ...Agonist-induced GPCR phosphorylation is a key determinant for the binding and activation of β-arrestins (βarrs). However, it is not entirely clear how different GPCRs harboring divergent phosphorylation patterns impart converging active conformation on βarrs leading to broadly conserved functional responses such as desensitization, endocytosis, and signaling. Here, we present multiple cryo-EM structures of activated βarrs in complex with distinct phosphorylation patterns derived from the carboxyl terminus of different GPCRs. These structures help identify a P-X-P-P type phosphorylation motif in GPCRs that interacts with a spatially organized K-K-R-R-K-K sequence in the N-domain of βarrs. Sequence analysis of the human GPCRome reveals the presence of this phosphorylation pattern in a large number of receptors, and its contribution in βarr activation is demonstrated by targeted mutagenesis experiments combined with an intrabody-based conformational sensor. Taken together, our findings provide important structural insights into the ability of distinct GPCRs to activate βarrs through a significantly conserved mechanism. #1: ![]() タイトル: Structure of beta-arrestin in complex with a phosphopeptide 著者: Maharana, J. / Sarma, P. / Yadav, M.K. / Banerjee, R. / Shukla, A.K. | ||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 268.9 KB | 表示 | ![]() |
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PDB形式 | ![]() | 214.6 KB | 表示 | ![]() |
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-検証レポート
文書・要旨 | ![]() | 1.3 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.3 MB | 表示 | |
XML形式データ | ![]() | 58.4 KB | 表示 | |
CIF形式データ | ![]() | 83.7 KB | 表示 | |
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-関連構造データ
関連構造データ | ![]() 34188MC ![]() 8go8C ![]() 8gocC ![]() 8gooC ![]() 8i0nC ![]() 8i0qC ![]() 8i0zC ![]() 8i10C 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 ( |
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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: 47088.508 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #2: タンパク質・ペプチド | 分子量: 2380.530 Da / 分子数: 2 / 由来タイプ: 合成 / 由来: (合成) ![]() #3: 抗体 | 分子量: 25512.354 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #4: 抗体 | 分子量: 23435.064 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() 研究の焦点であるリガンドがあるか | Y | |
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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 |
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分子量 | 値: 0.19 MDa / 実験値: YES | ||||||||||||||||||||||||||||||
由来(天然) |
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由来(組換発現) |
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緩衝液 | pH: 7.4 | ||||||||||||||||||||||||||||||
緩衝液成分 |
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試料 | 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: COPPER / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R2/2 | ||||||||||||||||||||||||||||||
急速凍結 | 装置: LEICA EM GP / 凍結剤: ETHANE / 湿度: 90 % / 凍結前の試料温度: 283.15 K / 詳細: Blotted for 3 seconds before plunging. |
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電子顕微鏡撮影
顕微鏡 | モデル: TFS GLACIOS |
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電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 46000 X / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 500 nm / Cs: 2.7 mm / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN |
撮影 | 電子線照射量: 49.3 e/Å2 / 検出モード: COUNTING / フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 実像数: 5637 |
画像スキャン | 動画フレーム数/画像: 40 |
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解析
EMソフトウェア |
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||||||||||
粒子像の選択 | 選択した粒子像数: 3236193 | ||||||||||||||||||||||||||||||||
対称性 | 点対称性: C2 (2回回転対称) | ||||||||||||||||||||||||||||||||
3次元再構成 | 解像度: 4.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 53387 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||||||
原子モデル構築 | プロトコル: FLEXIBLE FIT / 空間: REAL | ||||||||||||||||||||||||||||||||
原子モデル構築 | PDB-ID: 8GO8 Accession code: 8GO8 / Source name: PDB / タイプ: experimental model |