+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-21415 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
タイトル | Head region of the open conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. | |||||||||
マップデータ | Focused refinement | |||||||||
試料 |
| |||||||||
キーワード | Type 1 insulin-like growth factor receptor / Insulin-like growth factor II / ectodomain receptor / tyrosine kinase / SIGNALING PROTEIN | |||||||||
機能・相同性 | 機能・相同性情報 spongiotrophoblast cell proliferation / cardiac atrium development / negative regulation of cholangiocyte apoptotic process / negative regulation of muscle cell differentiation / positive regulation of skeletal muscle tissue growth / embryonic placenta morphogenesis / regulation of muscle cell differentiation / protein kinase complex / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process ...spongiotrophoblast cell proliferation / cardiac atrium development / negative regulation of cholangiocyte apoptotic process / negative regulation of muscle cell differentiation / positive regulation of skeletal muscle tissue growth / embryonic placenta morphogenesis / regulation of muscle cell differentiation / protein kinase complex / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / insulin-like growth factor binding / IRS-related events triggered by IGF1R / protein transporter activity / genomic imprinting / negative regulation of muscle cell apoptotic process / cellular response to progesterone stimulus / positive regulation of organ growth / positive regulation of DNA metabolic process / nitrogen catabolite activation of transcription from RNA polymerase II promoter / FCERI mediated MAPK activation / protein localization to nuclear periphery / cellular response to aldosterone / Activation of the AP-1 family of transcription factors / cellular response to zinc ion starvation / response to amino acid starvation / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / mediator complex binding / exocrine pancreas development / insulin receptor complex / insulin-like growth factor I binding / cellular response to testosterone stimulus / insulin receptor activity / transcytosis / negative regulation of hepatocyte apoptotic process / positive regulation of multicellular organism growth / alphav-beta3 integrin-IGF-1-IGF1R complex / Oxidative Stress Induced Senescence / response to alkaloid / cellular response to angiotensin / positive regulation of protein-containing complex disassembly / positive regulation of vascular endothelial cell proliferation / dendritic spine maintenance / insulin binding / response to L-glutamate / cellular response to insulin-like growth factor stimulus / establishment of cell polarity / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of cytokinesis / positive regulation of axon regeneration / positive regulation of activated T cell proliferation / positive regulation of osteoblast proliferation / positive regulation of cell division / TFIID-class transcription factor complex binding / amyloid-beta clearance / Respiratory syncytial virus (RSV) attachment and entry / regulation of JNK cascade / amino acid biosynthetic process / insulin receptor substrate binding / positive regulation of glycogen biosynthetic process / positive regulation of RNA polymerase II transcription preinitiation complex assembly / G-protein alpha-subunit binding / embryonic placenta development / response to vitamin E / estrous cycle / positive regulation of transcription initiation by RNA polymerase II / negative regulation of MAPK cascade / SHC-related events triggered by IGF1R / cellular response to nutrient levels / phosphatidylinositol 3-kinase binding / peptidyl-tyrosine autophosphorylation / positive regulation of insulin receptor signaling pathway / cellular response to transforming growth factor beta stimulus / striated muscle cell differentiation / insulin-like growth factor receptor binding / T-tubule / cellular response to amino acid starvation / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of mitotic nuclear division / axonogenesis / cellular response to dexamethasone stimulus / protein serine/threonine kinase activator activity / cerebellum development / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / hippocampus development / cellular response to estradiol stimulus / response to nicotine / animal organ morphogenesis / cellular response to glucose stimulus / positive regulation of smooth muscle cell proliferation / insulin receptor binding / growth factor activity / receptor protein-tyrosine kinase / caveola / hormone activity / cellular response to mechanical stimulus / RNA polymerase II transcription regulator complex / osteoblast differentiation 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (パン酵母) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.21 Å | |||||||||
データ登録者 | Xu Y / Kirk NS | |||||||||
資金援助 | オーストラリア, 英国, 2件
| |||||||||
引用 | ジャーナル: Structure / 年: 2020 タイトル: How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor. 著者: Yibin Xu / Nicholas S Kirk / Hariprasad Venugopal / Mai B Margetts / Tristan I Croll / Jarrod J Sandow / Andrew I Webb / Carlie A Delaine / Briony E Forbes / Michael C Lawrence / 要旨: Human type 1 insulin-like growth factor receptor (IGF-1R) signals chiefly in response to the binding of insulin-like growth factor I. Relatively little is known about the role of insulin-like growth ...Human type 1 insulin-like growth factor receptor (IGF-1R) signals chiefly in response to the binding of insulin-like growth factor I. Relatively little is known about the role of insulin-like growth factor II signaling via IGF-1R, despite the affinity of insulin-like growth factor II for IGF-1R being within an order of magnitude of that of insulin-like growth factor I. Here, we describe the cryoelectron microscopy structure of insulin-like growth factor II bound to a leucine-zipper-stabilized IGF-1R ectodomain, determined in two conformations to a maximum average resolution of 3.2 Å. The two conformations differ in the relative separation of their respective points of membrane entry, and comparison with the structure of insulin-like growth factor I bound to IGF-1R reveals long-suspected differences in the way in which the critical C domain of the respective growth factors interact with IGF-1R. | |||||||||
履歴 |
|
-構造の表示
ムービー |
ムービービューア |
---|---|
構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_21415.map.gz | 230 MB | EMDBマップデータ形式 | |
---|---|---|---|---|
ヘッダ (付随情報) | emd-21415-v30.xml emd-21415.xml | 18.4 KB 18.4 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_21415.png | 22.3 KB | ||
Filedesc metadata | emd-21415.cif.gz | 7.1 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-21415 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21415 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_21415_validation.pdf.gz | 496.3 KB | 表示 | EMDB検証レポート |
---|---|---|---|---|
文書・詳細版 | emd_21415_full_validation.pdf.gz | 495.9 KB | 表示 | |
XML形式データ | emd_21415_validation.xml.gz | 6.9 KB | 表示 | |
CIF形式データ | emd_21415_validation.cif.gz | 8 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21415 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21415 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
---|---|
「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_21415.map.gz / 形式: CCP4 / 大きさ: 244.1 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
注釈 | Focused refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
|
-添付データ
-試料の構成要素
-全体 : Head region of the open-leg conformation of the human type 1 insu...
全体 | 名称: Head region of the open-leg conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. |
---|---|
要素 |
|
-超分子 #1: Head region of the open-leg conformation of the human type 1 insu...
超分子 | 名称: Head region of the open-leg conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II. タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2 |
---|---|
由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 250 KDa |
-超分子 #2: Insulin-like growth factor 1 receptor
超分子 | 名称: Insulin-like growth factor 1 receptor / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #1 |
---|---|
由来(天然) | 生物種: Homo sapiens (ヒト) |
-超分子 #3: Insulin-like growth factor II
超分子 | 名称: Insulin-like growth factor II / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #2 |
---|
-分子 #1: Leucine-zippered human type 1 insulin-like growth factor receptor...
分子 | 名称: Leucine-zippered human type 1 insulin-like growth factor receptor ectodomain タイプ: protein_or_peptide / ID: 1 / コピー数: 2 / 光学異性体: LEVO / EC番号: receptor protein-tyrosine kinase |
---|---|
由来(天然) | 生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (パン酵母) 株: ATCC 204508 / S288c |
分子量 | 理論値: 108.937242 KDa |
組換発現 | 生物種: Cricetulus griseus (モンゴルキヌゲネズミ) |
配列 | 文字列: EICGPGIDIR NDYQQLKRLE NCTVIEGYLH ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVI FEMTNLKDIG LYNLRNITRG AIRIEKNADL CYLSTVDWSL ILDAVSNNYI VGNKPPKECG DLCPGTMEEK P MCEKTTIN ...文字列: EICGPGIDIR NDYQQLKRLE NCTVIEGYLH ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVI FEMTNLKDIG LYNLRNITRG AIRIEKNADL CYLSTVDWSL ILDAVSNNYI VGNKPPKECG DLCPGTMEEK P MCEKTTIN NEYNYRCWTT NRCQKMCPST CGKRACTENN ECCHPECLGS CSAPDNDTAC VACRHYYYAG VCVPACPPNT YR FEGWRCV DRDFCANILS AESSDSEGFV IHDGECMQEC PSGFIRNGSQ SMYCIPCEGP CPKVCEEEKK TKTIDSVTSA QML QGCTIF KGNLLINIRR GNNIASELEN FMGLIEVVTG YVKIRHSHAL VSLSFLKNLR LILGEEQLEG NYSFYVLDNQ NLQQ LWDWD HRNLTIKAGK MYFAFNPKLC VSEIYRMEEV TGTKGRQSKG DINTRNNGER ASCESDVLHF TSTTTSKNRI IITWH RYRP PDYRDLISFT VYYKEAPFKN VTEYDGQDAC GSNSWNMVDV DLPPNKDVEP GILLHGLKPW TQYAVYVKAV TLTMVE NDH IRGAKSEILY IRTNASVPSI PLDVLSASNS SSQLIVKWNP PSLPNGNLSY YIVRWQRQPQ DGYLYRHNYC SKDKIPI RK YADGTIDIEE VTENPKTEVC GGEKGPCCAC PKTEAEKQAE KEEAEYRKVF ENFLHNSIFV PRPERKRRDV MQVANTTM S SRSRNTTAAD TYNITDPEEL ETEYPFFESR VDNKERTVIS NLRPFTLYRI DIHSCNHEAE KLGCSASNFV FARTMPAEG ADDIPGPVTW EPRPENSIFL KWPEPENPNG LILMYEIKYG SQVEDQRECV SRQEYRKYGG AKLNRLNPGN YTARIQATSL SGNGSWTDP VFFYVQAKTG YENFIHRMKQ LEDKVEELLS KNYHLENEVA RLKKLVGERS SSEQKLISEE DLN UniProtKB: Insulin-like growth factor 1 receptor, General control transcription factor GCN4 |
-分子 #2: Insulin-like growth factor II
分子 | 名称: Insulin-like growth factor II / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
---|---|
由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 7.484472 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR GIVEECCFRS CDLALLETYC ATPAKSE UniProtKB: Insulin-like growth factor II |
-分子 #3: 2-acetamido-2-deoxy-beta-D-glucopyranose
分子 | 名称: 2-acetamido-2-deoxy-beta-D-glucopyranose / タイプ: ligand / ID: 3 / コピー数: 4 / 式: NAG |
---|---|
分子量 | 理論値: 221.208 Da |
Chemical component information | ChemComp-NAG: |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
---|---|
解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
濃度 | 0.1 mg/mL | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
緩衝液 | pH: 7.5 構成要素:
| ||||||||||
グリッド | モデル: Quantifoil, UltrAuFoil, R1.2/1.3 / 材質: GOLD / メッシュ: 300 / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 30 sec. / 詳細: 15mA current | ||||||||||
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277 K / 装置: FEI VITROBOT MARK IV | ||||||||||
詳細 | IGFII:IGF-1R molar ratio 1.5:1 |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
---|---|
特殊光学系 | エネルギーフィルター - 名称: GIF Quantum LS |
撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: COUNTING / デジタル化 - 画像ごとのフレーム数: 1-50 / 撮影したグリッド数: 1 / 実像数: 4585 / 平均露光時間: 10.0 sec. / 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | C2レンズ絞り径: 50.0 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm |
試料ステージ | ホルダー冷却材: NITROGEN |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
+画像解析
-原子モデル構築 1
初期モデル | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
---|---|
詳細 | UCSF Chimera was used for the initial fitting and ISOLDE v 1.03b was using for flexible fitting. |
精密化 | 空間: REAL / プロトコル: FLEXIBLE FIT |
得られたモデル | PDB-6vwg: |