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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: 8sv1 | |||||||||||||||||||||||||||||||||
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タイトル | Caspase-1 complex with interleukin-18 | |||||||||||||||||||||||||||||||||
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![]() | HYDROLASE / IMMUNE SYSTEM / Innate immune / Complex | |||||||||||||||||||||||||||||||||
機能・相同性 | ![]() interleukin-18 receptor binding / caspase-1 / protease inhibitor complex / AIM2 inflammasome complex assembly / The AIM2 inflammasome / AIM2 inflammasome complex / IPAF inflammasome complex / Interleukin-18 signaling / The IPAF inflammasome / icosanoid biosynthetic process ...interleukin-18 receptor binding / caspase-1 / protease inhibitor complex / AIM2 inflammasome complex assembly / The AIM2 inflammasome / AIM2 inflammasome complex / IPAF inflammasome complex / Interleukin-18 signaling / The IPAF inflammasome / icosanoid biosynthetic process / NLRP1 inflammasome complex / positive regulation of tissue remodeling / canonical inflammasome complex / positive regulation of T-helper 1 cell cytokine production / positive regulation of T-helper 2 cell differentiation / positive regulation of interleukin-18 production / cytokine precursor processing / CARD domain binding / NLRP3 inflammasome complex / positive regulation of interleukin-13 production / interleukin-18-mediated signaling pathway / positive regulation of neuroinflammatory response / neutrophil activation / negative regulation of myoblast differentiation / osmosensory signaling pathway / Interleukin-1 processing / sleep / positive regulation of NK T cell proliferation / positive regulation of tumor necrosis factor-mediated signaling pathway / Interleukin-37 signaling / positive regulation of macrophage derived foam cell differentiation / natural killer cell activation / positive regulation of granulocyte macrophage colony-stimulating factor production / type 2 immune response / pattern recognition receptor signaling pathway / cysteine-type endopeptidase activator activity involved in apoptotic process / triglyceride homeostasis / positive regulation of tyrosine phosphorylation of STAT protein / T-helper 1 type immune response / natural killer cell mediated cytotoxicity / signaling receptor ligand precursor processing / TP53 Regulates Transcription of Caspase Activators and Caspases / pyroptotic inflammatory response / cytokine binding / Interleukin-10 signaling / positive regulation of interleukin-17 production / positive regulation of natural killer cell proliferation / positive regulation of activated T cell proliferation / protein autoprocessing / The NLRP3 inflammasome / Pyroptosis / establishment of skin barrier / regulation of cell adhesion / Purinergic signaling in leishmaniasis infection / positive regulation of chemokine production / positive regulation of smooth muscle cell proliferation / cholesterol homeostasis / protein maturation / positive regulation of interleukin-1 beta production / cytokine activity / NOD1/2 Signaling Pathway / cellular response to mechanical stimulus / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of NF-kappaB transcription factor activity / cellular response to type II interferon / kinase binding / SARS-CoV-1 activates/modulates innate immune responses / positive regulation of type II interferon production / positive regulation of inflammatory response / cytokine-mediated signaling pathway / cell-cell signaling / positive regulation of cold-induced thermogenesis / cellular response to lipopolysaccharide / regulation of inflammatory response / angiogenesis / Interleukin-4 and Interleukin-13 signaling / regulation of apoptotic process / endopeptidase activity / defense response to virus / microtubule / cell population proliferation / positive regulation of canonical NF-kappaB signal transduction / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / defense response to Gram-positive bacterium / defense response to bacterium / immune response / inflammatory response / cysteine-type endopeptidase activity / apoptotic process / nucleolus / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / proteolysis / extracellular space / extracellular region / identical protein binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||||||||||||||||||||||||||
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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: 3.5 Å | |||||||||||||||||||||||||||||||||
![]() | Dong, Y. / Pascal, D. / Jon, K. / Wu, H. | |||||||||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural transitions enable interleukin-18 maturation and signaling. 著者: Ying Dong / Jeffrey P Bonin / Pascal Devant / Zhuoyi Liang / Alexander I M Sever / Julian Mintseris / James M Aramini / Gang Du / Stephen P Gygi / Jonathan C Kagan / Lewis E Kay / Hao Wu / ![]() ![]() ![]() 要旨: Several interleukin-1 (IL-1) family members, including IL-1β and IL-18, require processing by inflammasome-associated caspases to unleash their activities. Here, we unveil, by cryoelectron ...Several interleukin-1 (IL-1) family members, including IL-1β and IL-18, require processing by inflammasome-associated caspases to unleash their activities. Here, we unveil, by cryoelectron microscopy (cryo-EM), two major conformations of the complex between caspase-1 and pro-IL-18. One conformation is similar to the complex of caspase-4 and pro-IL-18, with interactions at both the active site and an exosite (closed conformation), and the other only contains interactions at the active site (open conformation). Thus, pro-IL-18 recruitment and processing by caspase-1 is less dependent on the exosite than the active site, unlike caspase-4. Structure determination by nuclear magnetic resonance uncovers a compact fold of apo pro-IL-18, which is similar to caspase-1-bound pro-IL-18 but distinct from cleaved IL-18. Binding sites for IL-18 receptor and IL-18 binding protein are only formed upon conformational changes after pro-IL-18 cleavage. These studies show how pro-IL-18 is selected as a caspase-1 substrate, and why cleavage is necessary for its inflammatory activity. | |||||||||||||||||||||||||||||||||
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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 | ![]() | 150.4 KB | 表示 | ![]() |
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PDB形式 | ![]() | 116.9 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 | ![]() | 1.1 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.1 MB | 表示 | |
XML形式データ | ![]() | 33.8 KB | 表示 | |
CIF形式データ | ![]() | 48.3 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 | ![]() 40781MC ![]() 8urvC 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 ( |
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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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要素
#1: タンパク質 | 分子量: 16607.154 Da / 分子数: 2 / 断片: subunit P20 (UNP residues 120-297) / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #2: タンパク質 | 分子量: 10258.755 Da / 分子数: 2 / 断片: subunit P10 (UNP residues 317-404) / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #3: タンパク質 | 分子量: 21850.641 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() 参照: UniProt: Q14116 Has protein modification | N | |
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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 |
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試料調製
構成要素 | 名称: protein complex with interleukin / タイプ: COMPLEX / Entity ID: all / 由来: MULTIPLE SOURCES |
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分子量 | 値: 100 MDa / 実験値: YES |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 7.4 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
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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: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 1000 nm |
撮影 | 電子線照射量: 55 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
EMソフトウェア | 名称: PHENIX / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 260549 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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