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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: 3duh | ||||||
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タイトル | Structure of Interleukin-23 | ||||||
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![]() | 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 | ![]() 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 smooth muscle cell apoptotic process / positive regulation of NK T cell activation / positive regulation of T-helper 1 type immune response / sexual reproduction / positive regulation of mononuclear cell proliferation / interleukin-12 receptor binding / Interleukin-23 signaling / positive regulation of T-helper 17 type immune response / interleukin-12-mediated signaling pathway / positive regulation of NK T cell proliferation / T-helper cell differentiation / positive regulation of memory T cell differentiation / Interleukin-12 signaling / positive regulation of natural killer cell proliferation / positive regulation of osteoclast differentiation / negative regulation of interleukin-17 production / cell surface receptor signaling pathway via STAT / cytokine receptor activity / natural killer cell activation / response to UV-B / positive regulation of granulocyte macrophage colony-stimulating factor production / positive regulation of neutrophil chemotaxis / T-helper 1 type immune response / negative regulation of interleukin-10 production / defense response to protozoan / Interleukin-10 signaling / positive regulation of interleukin-17 production / positive regulation of activated T cell proliferation / positive regulation of interleukin-10 production / cell surface receptor signaling pathway via JAK-STAT / negative regulation of protein secretion / positive regulation of T-helper 17 cell lineage commitment / positive regulation of T cell proliferation / T cell proliferation / positive regulation of defense response to virus by host / positive regulation of interleukin-12 production / positive regulation of cell adhesion / regulation of cytokine production / cytokine activity / negative regulation of smooth muscle cell proliferation / negative regulation of inflammatory response to antigenic stimulus / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of T cell mediated cytotoxicity / cellular response to type II interferon / positive regulation of type II interferon production / positive regulation of inflammatory response / positive regulation of tumor necrosis factor production / cell migration / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / Interleukin-4 and Interleukin-13 signaling / defense response to virus / inflammatory response / endoplasmic reticulum lumen / protein heterodimerization activity / innate immune response / protein-containing complex binding / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / identical protein binding / membrane / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() ![]() ![]() | ||||||
![]() | Lupardus, P.J. / Garcia, K.C. | ||||||
![]() | ![]() 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: ![]() ![]() |
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ダウンロードとリンク
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PDBx/mmCIF形式 | ![]() | 186.3 KB | 表示 | ![]() |
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PDB形式 | ![]() | 146.7 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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 |
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リンク
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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) ![]() 発現宿主: ![]() ![]() 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) ![]() 発現宿主: ![]() ![]() 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: ![]() |
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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: ![]() ![]() ![]() |
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 |
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解析
ソフトウェア |
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精密化 | 構造決定の手法: ![]() 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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