+データを開く
-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 | ||||||
要素 |
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キーワード | 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 | 機能・相同性情報 glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / cardiac atrium development / proteoglycan biosynthetic process / negative regulation of cholangiocyte apoptotic process / positive regulation of glycoprotein biosynthetic process ...glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / cardiac atrium development / proteoglycan biosynthetic process / negative regulation of cholangiocyte apoptotic process / positive regulation of glycoprotein biosynthetic process / myotube cell development / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process / negative regulation of neuroinflammatory response / protein kinase complex / bone mineralization involved in bone maturation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / positive regulation of cell growth involved in cardiac muscle cell development / negative regulation of vascular associated smooth muscle cell apoptotic process / protein transporter activity / IRS-related events triggered by IGF1R / insulin-like growth factor binding / exocytic vesicle / regulation of female gonad development / negative regulation of muscle cell apoptotic process / cellular response to progesterone stimulus / positive regulation of meiotic cell cycle / positive regulation of DNA metabolic process / cellular response to zinc ion starvation / cellular response to aldosterone / positive regulation of developmental growth / cell activation / positive regulation of calcineurin-NFAT signaling cascade / insulin-like growth factor II binding / male sex determination / exocrine pancreas development / insulin receptor complex / cellular response to testosterone stimulus / negative regulation of hepatocyte apoptotic process / positive regulation of transcription regulatory region DNA binding / insulin-like growth factor I binding / insulin receptor activity / transcytosis / alphav-beta3 integrin-IGF-1-IGF1R complex / response to alkaloid / positive regulation of Ras protein signal transduction / cellular response to angiotensin / positive regulation of protein-containing complex disassembly / myoblast differentiation / positive regulation of insulin-like growth factor receptor signaling pathway / cargo receptor activity / myoblast proliferation / muscle organ development / negative regulation of interleukin-1 beta production / dendritic spine maintenance / cellular response to insulin-like growth factor stimulus / response to L-glutamate / insulin binding / PTB domain binding / negative regulation of MAPK cascade / adrenal gland development / establishment of cell polarity / neuronal cell body membrane / Signaling by Insulin receptor / IRS activation / activation of protein kinase activity / positive regulation of cardiac muscle hypertrophy / positive regulation of activated T cell proliferation / positive regulation of smooth muscle cell migration / positive regulation of axon regeneration / amyloid-beta clearance / negative regulation of release of cytochrome c from mitochondria / positive regulation of osteoblast proliferation / positive regulation of respiratory burst / positive regulation of cytokinesis / negative regulation of amyloid-beta formation / negative regulation of smooth muscle cell apoptotic process / Respiratory syncytial virus (RSV) attachment and entry / positive regulation of receptor internalization / regulation of embryonic development / regulation of JNK cascade / negative regulation of tumor necrosis factor production / transport across blood-brain barrier / insulin receptor substrate binding / estrous cycle / positive regulation of glycogen biosynthetic process / G-protein alpha-subunit binding / Synthesis, secretion, and deacylation of Ghrelin / response to vitamin E / epidermis development / epithelial to mesenchymal transition / positive regulation of DNA binding / SHC-related events triggered by IGF1R / Signal attenuation / positive regulation of osteoblast differentiation / phosphatidylinositol 3-kinase binding / heart morphogenesis / peptidyl-tyrosine autophosphorylation / positive regulation of tyrosine phosphorylation of STAT protein 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: 3.7 Å | ||||||
データ登録者 | Xu, Y. / Lawrence, M.C. | ||||||
資金援助 | オーストラリア, 1件
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引用 | ジャーナル: Structure / 年: 2022 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. | ||||||
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 | 7s0q.cif.gz | 349.6 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7s0q.ent.gz | 280.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 7s0q.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 | 7s0q_validation.pdf.gz | 1011.4 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7s0q_full_validation.pdf.gz | 1024 KB | 表示 | |
XML形式データ | 7s0q_validation.xml.gz | 34.8 KB | 表示 | |
CIF形式データ | 7s0q_validation.cif.gz | 50.1 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/s0/7s0q ftp://data.pdbj.org/pub/pdb/validation_reports/s0/7s0q | 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 (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
-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) Homo sapiens (ヒト) / 遺伝子: IGF1R / 細胞株 (発現宿主): CHO Lec8 発現宿主: Cricetulus griseus (モンゴルキヌゲネズミ) 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) Homo sapiens (ヒト) / 遺伝子: IGF1, IBP1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P05019 |
-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) Homo sapiens (ヒト) / 遺伝子: INSR / 細胞株 (発現宿主): CHO lek8 発現宿主: Cricetulus griseus (モンゴルキヌゲネズミ) 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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-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: 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: Homo sapiens (ヒト) |
由来(組換発現) | 生物種: Cricetulus griseus (モンゴルキヌゲネズミ) |
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 |
-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: OTHER |
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) |
-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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