+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 3duh | ||||||
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タイトル | Structure of Interleukin-23 | ||||||
要素 |
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キーワード | IMMUNE SYSTEM/CYTOKINE / four-helix bundle cytokine / Ig domain / Cytokine / Glycoprotein / Immunoglobulin domain / Secreted / Antiviral defense / Immune response / Inflammatory response / Innate immunity / Tissue remodeling / IMMUNE SYSTEM / IMMUNE SYSTEM-CYTOKINE COMPLEX | ||||||
機能・相同性 | 機能・相同性情報 late endosome lumen / interleukin-23 receptor binding / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of natural killer cell activation / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis ...late endosome lumen / interleukin-23 receptor binding / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of natural killer cell activation / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of lymphocyte proliferation / positive regulation of tissue remodeling / tissue remodeling / positive regulation of T-helper 1 type immune response / sexual reproduction / positive regulation of NK T cell activation / positive regulation of smooth muscle cell apoptotic process / positive regulation of mononuclear cell proliferation / interleukin-12 receptor binding / positive regulation of memory T cell differentiation / T-helper cell differentiation / natural killer cell activation / Interleukin-23 signaling / CD22 mediated BCR regulation / positive regulation of T-helper 17 type immune response / positive regulation of osteoclast differentiation / interleukin-12-mediated signaling pathway / negative regulation of interleukin-17 production / positive regulation of NK T cell proliferation / positive regulation of neutrophil chemotaxis / Interleukin-12 signaling / response to UV-B / positive regulation of natural killer cell proliferation / positive regulation of granulocyte macrophage colony-stimulating factor production / cytokine receptor activity / Fc epsilon receptor (FCERI) signaling / T-helper 1 type immune response / Classical antibody-mediated complement activation / negative regulation of interleukin-10 production / Initial triggering of complement / defense response to protozoan / positive regulation of activated T cell proliferation / cytokine binding / positive regulation of interleukin-17 production / Interleukin-10 signaling / immunoglobulin complex / cell surface receptor signaling pathway via JAK-STAT / positive regulation of interleukin-10 production / FCGR activation / negative regulation of protein secretion / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / positive regulation of defense response to virus by host / Scavenging of heme from plasma / positive regulation of T-helper 17 cell lineage commitment / positive regulation of T cell proliferation / T cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / regulation of cytokine production / positive regulation of interleukin-12 production / antigen binding / positive regulation of cell adhesion / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Regulation of Complement cascade / cytokine activity / negative regulation of inflammatory response to antigenic stimulus / Cell surface interactions at the vascular wall / FCGR3A-mediated phagocytosis / FCERI mediated MAPK activation / negative regulation of smooth muscle cell proliferation / cellular response to type II interferon / cytokine-mediated signaling pathway / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / positive regulation of inflammatory response / positive regulation of T cell mediated cytotoxicity / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of type II interferon production / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of tumor necrosis factor production / cell migration / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / defense response to virus / defense response to Gram-negative bacterium / blood microparticle / adaptive immune response / Potential therapeutics for SARS / receptor complex / inflammatory response / immune response / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / innate immune response / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / extracellular space 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.3 Å | ||||||
データ登録者 | Lupardus, P.J. / Garcia, K.C. | ||||||
引用 | ジャーナル: J.Mol.Biol. / 年: 2008 タイトル: The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12. 著者: Lupardus, P.J. / Garcia, K.C. | ||||||
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 | 3duh.cif.gz | 186.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb3duh.ent.gz | 146.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 3duh.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 | 3duh_validation.pdf.gz | 483 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 3duh_full_validation.pdf.gz | 498.2 KB | 表示 | |
XML形式データ | 3duh_validation.xml.gz | 34.3 KB | 表示 | |
CIF形式データ | 3duh_validation.cif.gz | 48.6 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/du/3duh ftp://data.pdbj.org/pub/pdb/validation_reports/du/3duh | HTTPS FTP |
-関連構造データ
関連構造データ | 1f45S S: 精密化の開始モデル |
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類似構造データ |
-リンク
-集合体
登録構造単位 |
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単位格子 |
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-要素
#1: 抗体 | 分子量: 35811.086 Da / 分子数: 2 / 由来タイプ: 組換発現 詳細: Gp67 signal sequence at N-terminus and 6xHis tag at C-terminus 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: IL12B, NKSF2 / プラスミド: pACSG2 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 株 (発現宿主): HiFive / 参照: UniProt: P29460 #2: タンパク質 | 分子量: 19638.164 Da / 分子数: 2 / 由来タイプ: 組換発現 詳細: Gp67 signal sequence at N-terminus and 6xHis tag at C-terminus 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: IL23A, SGRF, UNQ2498/PRO5798 / プラスミド: pACSG2 発現宿主: Spodoptera frugiperda (ツマジロクサヨトウ) 株 (発現宿主): HiFive / 参照: UniProt: Q9NPF7 #3: 糖 | #4: 水 | ChemComp-HOH / | Has protein modification | Y | |
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-実験情報
-実験
実験 | 手法: X線回折 / 使用した結晶の数: 1 |
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-試料調製
結晶 | マシュー密度: 2.52 Å3/Da / 溶媒含有率: 51.13 % |
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結晶化 | 温度: 295 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 7 詳細: 20% PEG3350, 0.2M potassium nitrate, 0.1M Hepes-NaOH pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-データ収集
回折 | 平均測定温度: 140 K |
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放射光源 | 由来: シンクロトロン / サイト: SSRL / ビームライン: BL11-1 / 波長: 1 Å |
検出器 | タイプ: MARMOSAIC 325 mm CCD / 検出器: CCD / 日付: 2008年5月4日 |
放射 | モノクロメーター: Si(111), Side scattering bent cube-root I-beam single crystal; asymmetric cut 4.965 degs プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 1 Å / 相対比: 1 |
反射 | 解像度: 2.3→30 Å / Num. obs: 49424 / % possible obs: 99.9 % / 冗長度: 3.7 % / Biso Wilson estimate: 47.1 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 13.6 |
反射 シェル | 解像度: 2.3→2.42 Å / 冗長度: 3.7 % / Rmerge(I) obs: 0.556 / Mean I/σ(I) obs: 2.5 / Num. unique all: 7208 / % possible all: 100 |
-解析
ソフトウェア |
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精密化 | 構造決定の手法: 分子置換 開始モデル: human p40 from PDB ID 1F45 解像度: 2.3→30 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.915 / SU B: 7.997 / SU ML: 0.196 / 交差検証法: THROUGHOUT / ESU R: 0.325 / ESU R Free: 0.243 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD / 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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溶媒の処理 | イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 46.587 Å2
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精密化ステップ | サイクル: LAST / 解像度: 2.3→30 Å
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拘束条件 |
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LS精密化 シェル | 解像度: 2.3→2.359 Å / Total num. of bins used: 20
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