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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: 6jxr | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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タイトル | Structure of human T cell receptor-CD3 complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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![]() | IMMUNE SYSTEM | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
機能・相同性 | ![]() regulation of lymphocyte apoptotic process / gamma-delta T cell receptor complex / Fc-gamma receptor III complex / T cell anergy / positive regulation of cell-cell adhesion mediated by integrin / T cell activation involved in immune response / positive regulation of T cell anergy / gamma-delta T cell activation / Fc-gamma receptor signaling pathway / CD4-positive, alpha-beta T cell proliferation ...regulation of lymphocyte apoptotic process / gamma-delta T cell receptor complex / Fc-gamma receptor III complex / T cell anergy / positive regulation of cell-cell adhesion mediated by integrin / T cell activation involved in immune response / positive regulation of T cell anergy / gamma-delta T cell activation / Fc-gamma receptor signaling pathway / CD4-positive, alpha-beta T cell proliferation / negative thymic T cell selection / positive regulation of CD4-positive, alpha-beta T cell proliferation / alpha-beta T cell receptor complex / positive regulation of protein localization to cell surface / positive thymic T cell selection / signal complex assembly / Nef and signal transduction / positive regulation of cell-matrix adhesion / T cell receptor complex / smoothened signaling pathway / establishment or maintenance of cell polarity / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / positive regulation of interleukin-4 production / dendrite development / protein complex oligomerization / alpha-beta T cell activation / Generation of second messenger molecules / FCGR activation / immunological synapse / Co-inhibition by PD-1 / Role of phospholipids in phagocytosis / T cell receptor binding / positive regulation of T cell proliferation / T cell costimulation / positive regulation of interleukin-2 production / cerebellum development / endomembrane system / FCGR3A-mediated IL10 synthesis / positive regulation of calcium-mediated signaling / T cell activation / cell surface receptor protein tyrosine kinase signaling pathway / protein tyrosine kinase binding / negative regulation of smoothened signaling pathway / FCGR3A-mediated phagocytosis / response to bacterium / apoptotic signaling pathway / clathrin-coated endocytic vesicle membrane / calcium-mediated signaling / peptide antigen binding / Regulation of actin dynamics for phagocytic cup formation / SH3 domain binding / positive regulation of type II interferon production / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / transmembrane signaling receptor activity / Downstream TCR signaling / cell-cell junction / protein transport / Cargo recognition for clathrin-mediated endocytosis / signaling receptor complex adaptor activity / T cell receptor signaling pathway / Clathrin-mediated endocytosis / cell body / protein-containing complex assembly / regulation of apoptotic process / dendritic spine / adaptive immune response / cell surface receptor signaling pathway / G protein-coupled receptor signaling pathway / protein heterodimerization activity / external side of plasma membrane / negative regulation of gene expression / positive regulation of gene expression / protein kinase binding / cell surface / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
生物種 | ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / ネガティブ染色法 / クライオ電子顕微鏡法 / 解像度: 3.7 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Dong, D. / Zheng, L. / Lin, J. / Zhu, Y. / Li, N. / Zhang, B. / Xie, S. / Zheng, J. / Wang, Y. / Gao, N. / Huang, Z. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural basis of assembly of the human T cell receptor-CD3 complex. 著者: De Dong / Lvqin Zheng / Jianquan Lin / Bailing Zhang / Yuwei Zhu / Ningning Li / Shuangyu Xie / Yuhang Wang / Ning Gao / Zhiwei Huang / ![]() 要旨: The αβ T cell receptor (TCR), in association with the CD3γε-CD3δε-CD3ζζ signalling hexamer, is the primary determinant of T cell development and activation, and of immune responses to foreign ...The αβ T cell receptor (TCR), in association with the CD3γε-CD3δε-CD3ζζ signalling hexamer, is the primary determinant of T cell development and activation, and of immune responses to foreign antigens. The mechanism of assembly of the TCR-CD3 complex remains unknown. Here we report a cryo-electron microscopy structure of human TCRαβ in complex with the CD3 hexamer at 3.7 Å resolution. The structure contains the complete extracellular domains and all the transmembrane helices of TCR-CD3. The octameric TCR-CD3 complex is assembled with 1:1:1:1 stoichiometry of TCRαβ:CD3γε:CD3δε:CD3ζζ. Assembly of the extracellular domains of TCR-CD3 is mediated by the constant domains and connecting peptides of TCRαβ that pack against CD3γε-CD3δε, forming a trimer-like structure proximal to the plasma membrane. The transmembrane segment of the CD3 complex adopts a barrel-like structure formed by interaction of the two transmembrane helices of CD3ζζ with those of CD3γε and CD3δε. Insertion of the transmembrane helices of TCRαβ into the barrel-like structure via both hydrophobic and ionic interactions results in transmembrane assembly of the TCR-CD3 complex. Together, our data reveal the structural basis for TCR-CD3 complex assembly, providing clues to TCR triggering and a foundation for rational design of immunotherapies that target the complex. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
履歴 |
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構造の表示
ムービー |
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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 | ![]() | 209.1 KB | 表示 | ![]() |
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PDB形式 | ![]() | 159.4 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 | ![]() | 900.3 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 908.9 KB | 表示 | |
XML形式データ | ![]() | 33.4 KB | 表示 | |
CIF形式データ | ![]() | 52.4 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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要素
-T-cell surface glycoprotein CD3 ... , 4種, 6分子 abdfeg
#1: タンパク質 | 分子量: 18723.439 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #2: タンパク質 | | 分子量: 18949.537 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #3: タンパク質 | 分子量: 23174.227 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #4: タンパク質 | | 分子量: 20493.457 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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-T cell receptor ... , 2種, 2分子 mn
#5: タンパク質 | 分子量: 28308.662 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: fusion protein of residues 22-114 from A0A0B4J271, residues 116-132 from A0N4Z6 and residues 134-273 from P01848. 由来: (組換発現) ![]() ![]() 参照: UniProt: A0A0B4J271, UniProt: A0N4Z6, UniProt: P01848 |
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#6: タンパク質 | 分子量: 32498.463 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: fusion protein of residues 22-112 from A0A0K0K1A5, residues 121-134 from P0DSE2 and residues 135-312 from A0A0G2JMB4. 由来: (組換発現) ![]() ![]() 参照: UniProt: A0A0K0K1A5, UniProt: P0DSE2, UniProt: A0A0G2JMB4 |
-詳細
Has protein modification | Y |
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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: CELL / 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: complex / タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 7.5 |
試料 | 包埋: NO / シャドウイング: NO / 染色: YES / 凍結: YES |
染色 | タイプ: NEGATIVE / 染色剤: Uranyl Acetate |
急速凍結 | 凍結剤: NITROGEN |
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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: DARK FIELD |
撮影 | 電子線照射量: 64.4 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.13_2998: / 分類: 精密化 | ||||||||||||||||||||||||
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EMソフトウェア | 名称: PHENIX / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 197487 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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