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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: 7al7 | ||||||
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タイトル | The Crystal Structure of Human IL-18 in Complex With Human IL-18 Binding Protein | ||||||
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![]() | CYTOKINE / decoy receptor / antagonist / complex | ||||||
機能・相同性 | ![]() interleukin-18 binding / interleukin-18 receptor binding / Interleukin-18 signaling / positive regulation of tissue remodeling / receptor antagonist activity / positive regulation of T-helper 2 cell differentiation / positive regulation of T-helper 1 cell cytokine production / positive regulation of macrophage derived foam cell differentiation / positive regulation of interleukin-13 production / positive regulation of neuroinflammatory response ...interleukin-18 binding / interleukin-18 receptor binding / Interleukin-18 signaling / positive regulation of tissue remodeling / receptor antagonist activity / positive regulation of T-helper 2 cell differentiation / positive regulation of T-helper 1 cell cytokine production / positive regulation of macrophage derived foam cell differentiation / positive regulation of interleukin-13 production / positive regulation of neuroinflammatory response / interleukin-18-mediated signaling pathway / natural killer cell mediated cytotoxicity / negative regulation of myoblast differentiation / type 2 immune response / natural killer cell activation / sleep / neutrophil activation / Interleukin-1 processing / positive regulation of NK T cell proliferation / Interleukin-37 signaling / triglyceride homeostasis / positive regulation of granulocyte macrophage colony-stimulating factor production / positive regulation of natural killer cell proliferation / T-helper 1 type immune response / positive regulation of activated T cell proliferation / positive regulation of interleukin-17 production / Interleukin-10 signaling / glutathione transferase / glutathione transferase activity / establishment of skin barrier / Pyroptosis / regulation of cell adhesion / Purinergic signaling in leishmaniasis infection / positive regulation of chemokine production / positive regulation of tyrosine phosphorylation of STAT protein / glutathione metabolic process / cytokine activity / cholesterol homeostasis / positive regulation of smooth muscle cell proliferation / cellular response to hydrogen peroxide / positive regulation of inflammatory response / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of type II interferon production / cell-cell signaling / cellular response to tumor necrosis factor / positive regulation of cold-induced thermogenesis / positive regulation of NF-kappaB transcription factor activity / cellular response to lipopolysaccharide / angiogenesis / Interleukin-4 and Interleukin-13 signaling / cell population proliferation / response to lipopolysaccharide / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / defense response to Gram-positive bacterium / inflammatory response / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() | ||||||
手法 | ![]() ![]() ![]() | ||||||
![]() | Detry, S. / Andries, J. / Bloch, Y. / Clancy, D. / Savvides, S.N. | ||||||
資金援助 | European Union, 1件
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![]() | ![]() タイトル: Structural basis of human IL-18 sequestration by the decoy receptor IL-18 binding protein in inflammation and tumor immunity. 著者: Detry, S. / Andries, J. / Bloch, Y. / Gabay, C. / Clancy, D.M. / Savvides, S.N. | ||||||
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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 | ![]() | 179.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 139.4 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 | ![]() | 463.6 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 464.8 KB | 表示 | |
XML形式データ | ![]() | 13.4 KB | 表示 | |
CIF形式データ | ![]() | 18.7 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 | ![]() 3f62S S: 精密化の開始モデル |
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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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単位格子 |
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要素
#1: タンパク質 | 分子量: 18749.832 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: The final protein sequence used for crystallization starts at T30 and ends at D170. The N-terminal RTPmu signal sequence is cleaved during expression. The C-terminal AVI-HIS tag was cleaved ...詳細: The final protein sequence used for crystallization starts at T30 and ends at D170. The N-terminal RTPmu signal sequence is cleaved during expression. The C-terminal AVI-HIS tag was cleaved by caspase-3 after the DEVD site. In reference to the native sequence, the final protein sequence starts at Q63 and ends at G194, as it lacks an N-terminal region from T31 to K62. 由来: (組換発現) ![]() ![]() | ||||
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#2: タンパク質 | 分子量: 45695.297 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. ...詳細: The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193,The protein was expressed as a HIS-GST fusion which was cleaved after the DEVD site using caspasea-3. Thus, the final protein sequence used for crystallization starts at Y234 and ends at D390. In reference to the native sequence, the final protein sequence starts at Y37 and ends at D193 由来: (組換発現) ![]() ![]() ![]() プラスミド: pET-42 / 遺伝子: IL18, IGIF, IL1F4 / 詳細 (発現宿主): HIS-GST tag added N-terminally / 発現宿主: ![]() ![]() 参照: UniProt: P08515, UniProt: Q14116, glutathione transferase | ||||
#3: 糖 | #4: 水 | ChemComp-HOH / | 研究の焦点であるリガンドがあるか | N | |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶化 | 温度: 293 K / 手法: 蒸気拡散法 / pH: 6.5 詳細: 0.2 M Calcium acetate hydrate, 0.1 M Sodium cacodylate trihydrate pH 6.5, 18% w/v Polyethylene glycol 8000 Temp details: Room temperature |
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-データ収集
回折 | 平均測定温度: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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放射光源 | 由来: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
検出器 | タイプ: DECTRIS EIGER X 16M / 検出器: PIXEL / 日付: 2019年5月24日 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
放射 | 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: 0.9762 Å / 相対比: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
反射 | 解像度: 1.8→59.39 Å / Num. obs: 26507 / % possible obs: 98.27 % / 冗長度: 6.9 % / CC1/2: 0.999 / CC star: 1 / Rmerge(I) obs: 0.048 / Rpim(I) all: 0.02 / Rrim(I) all: 0.053 / Net I/σ(I): 15.67 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
反射 シェル |
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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: 3F62 解像度: 1.801→59.386 Å / SU ML: 0.29 / 交差検証法: THROUGHOUT / σ(F): 1.36 / 位相誤差: 39.86 / 立体化学のターゲット値: ML
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溶媒の処理 | 減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso max: 184.21 Å2 / Biso mean: 38.4789 Å2 / Biso min: 5.01 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: final / 解像度: 1.801→59.386 Å
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LS精密化 シェル | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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