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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: 7s0q | ||||||
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タイトル | Head region of a complex of IGF-I with the ectodomain of a hybrid insulin receptor / type 1 insulin-like growth factor receptor | ||||||
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![]() | SIGNALING PROTEIN / insulin receptor / type 1 insulin like growth factor receptor / hybrid receptor / insulin like growth factor I / leucine zipper / cryo electron microscopy | ||||||
機能・相同性 | ![]() glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / positive regulation of trophectodermal cell proliferation / prostate gland stromal morphogenesis / positive regulation of type B pancreatic cell proliferation / positive regulation of glycoprotein biosynthetic process / type II pneumocyte differentiation ...glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / positive regulation of trophectodermal cell proliferation / prostate gland stromal morphogenesis / positive regulation of type B pancreatic cell proliferation / positive regulation of glycoprotein biosynthetic process / type II pneumocyte differentiation / neuronal dense core vesicle lumen / proteoglycan biosynthetic process / regulation of establishment or maintenance of cell polarity / chondroitin sulfate proteoglycan biosynthetic process / protein kinase complex / insulin-like growth factor receptor activity / myotube cell development / positive regulation of transcription regulatory region DNA binding / negative regulation of neuroinflammatory response / insulin-like growth factor binding / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / bone mineralization involved in bone maturation / protein transporter activity / positive regulation of cell growth involved in cardiac muscle cell development / IRS-related events triggered by IGF1R / negative regulation of vascular associated smooth muscle cell apoptotic process / positive regulation of cerebellar granule cell precursor proliferation / exocytic vesicle / lung vasculature development / regulation of female gonad development / transcytosis / cerebellar granule cell precursor proliferation / positive regulation of myoblast proliferation / positive regulation of meiotic cell cycle / lung lobe morphogenesis / positive regulation of myelination / negative regulation of androgen receptor signaling pathway / cell activation / insulin-like growth factor II binding / positive regulation of developmental growth / glial cell differentiation / positive regulation of calcineurin-NFAT signaling cascade / male sex determination / insulin receptor complex / prostate gland growth / transmembrane receptor protein tyrosine kinase activator activity / insulin-like growth factor I binding / positive regulation of protein-containing complex disassembly / type B pancreatic cell proliferation / insulin receptor activity / mammary gland development / exocrine pancreas development / alphav-beta3 integrin-IGF-1-IGF1R complex / myoblast differentiation / cell surface receptor signaling pathway via STAT / positive regulation of Ras protein signal transduction / regulation of nitric oxide biosynthetic process / regulation of JNK cascade / positive regulation of insulin-like growth factor receptor signaling pathway / dendritic spine maintenance / cargo receptor activity / positive regulation of smooth muscle cell migration / peptidyl-tyrosine autophosphorylation / insulin binding / growth hormone receptor signaling pathway / positive regulation of DNA binding / negative regulation of interleukin-1 beta production / adrenal gland development / neuronal cell body membrane / PTB domain binding / lung alveolus development / muscle organ development / cellular response to insulin-like growth factor stimulus / Signaling by Insulin receptor / IRS activation / positive regulation of cardiac muscle hypertrophy / branching morphogenesis of an epithelial tube / androgen receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / negative regulation of release of cytochrome c from mitochondria / type I pneumocyte differentiation / negative regulation of amyloid-beta formation / negative regulation of smooth muscle cell apoptotic process / positive regulation of respiratory burst / amyloid-beta clearance / positive regulation of activated T cell proliferation / inner ear development / Respiratory syncytial virus (RSV) attachment and entry / myoblast proliferation / positive regulation of receptor internalization / regulation of embryonic development / insulin receptor substrate binding / negative regulation of tumor necrosis factor production / protein kinase activator activity / epithelial to mesenchymal transition / blood vessel remodeling / Synthesis, secretion, and deacylation of Ghrelin / epidermis development / activation of protein kinase B activity 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: 3.7 Å | ||||||
![]() | Xu, Y. / Lawrence, M.C. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: How insulin-like growth factor I binds to a hybrid insulin receptor type 1 insulin-like growth factor receptor. 著者: Yibin Xu / Mai B Margetts / Hari Venugopal / John G Menting / Nicholas S Kirk / Tristan I Croll / Carlie Delaine / Briony E Forbes / Michael C Lawrence / ![]() ![]() 要旨: Monomers of the insulin receptor and type 1 insulin-like growth factor receptor (IGF-1R) can combine stochastically to form heterodimeric hybrid receptors. These hybrid receptors display ligand ...Monomers of the insulin receptor and type 1 insulin-like growth factor receptor (IGF-1R) can combine stochastically to form heterodimeric hybrid receptors. These hybrid receptors display ligand binding and signaling properties that differ from those of the homodimeric receptors. Here, we describe the cryoelectron microscopy structure of such a hybrid receptor in complex with insulin-like growth factor I (IGF-I). The structure (ca. 3.7 Å resolution) displays a single IGF-I ligand, bound in a similar fashion to that seen for IGFs in complex with IGF-1R. The IGF-I ligand engages the first leucine-rich-repeat domain and cysteine-rich region of the IGF-1R monomer (rather than those of the insulin receptor monomer), consistent with the determinants for IGF binding residing in the IGF-1R cysteine-rich region. The structure broadens our understanding of this receptor family and assists in delineating the key structural motifs involved in binding their respective ligands. | ||||||
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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 | ![]() | 357 KB | 表示 | ![]() |
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PDB形式 | ![]() | 280.2 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 | ![]() | 1.1 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.1 MB | 表示 | |
XML形式データ | ![]() | 34.4 KB | 表示 | |
CIF形式データ | ![]() | 49.9 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 | ![]() 24791MC ![]() 7s8vC 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
-Insulin-like growth factor ... , 2種, 2分子 AD
#1: タンパク質 | 分子量: 108937.242 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: P08069, receptor protein-tyrosine kinase |
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#3: タンパク質 | 分子量: 7663.752 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
-タンパク質 , 1種, 1分子 B
#2: タンパク質 | 分子量: 109809.617 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: P06213, receptor protein-tyrosine kinase |
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-糖 , 4種, 11分子 


#4: 多糖 | #5: 多糖 | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | #6: 糖 | ChemComp-BMA / | #7: 糖 | ChemComp-NAG / |
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-詳細
研究の焦点であるリガンドがあるか | Y |
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Has protein modification | 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 |
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試料調製
構成要素 | 名称: a complex of IGF-I with the ectodomain of a hybrid insulin receptor / type 1 insulin-like growth factor receptor タイプ: COMPLEX / Entity ID: #1-#3 / 由来: MULTIPLE SOURCES |
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分子量 | 値: 250 kDa/nm / 実験値: YES |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 8 / 詳細: 20mM Tris pH 8.0 160mM NaCl |
緩衝液成分 | 濃度: 20 mM / 名称: TRIS / 式: C4H11NO3 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES / 詳細: 0.2mg/ml |
試料支持 | グリッドの材料: COPPER |
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE |
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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: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 1.44 e/Å2 / 検出モード: COUNTING フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.17_3644: / 分類: 精密化 | ||||||||||||||||||||||||||||
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EMソフトウェア |
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||||||
3次元再構成 | 解像度: 3.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 151240 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: REAL | ||||||||||||||||||||||||||||
拘束条件 |
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