- EMDB-28573: CryoEM structure of HLA-A2 bound to MAGEA4 (230-239) peptide -
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IDまたはキーワード:
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基本情報
登録情報
データベース: EMDB / ID: EMD-28573
タイトル
CryoEM structure of HLA-A2 bound to MAGEA4 (230-239) peptide
マップデータ
試料
複合体: Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microglobulin, MAGE-A4 peptide in complex with anti-Beta-2-microglobulin Fab 2M2
タンパク質・ペプチド: Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera
キーワード
HLA / MHC / IMMUNE SYSTEM
機能・相同性
機能・相同性情報
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / lumenal side of endoplasmic reticulum membrane / ER to Golgi transport vesicle membrane / positive regulation of T cell mediated cytotoxicity / recycling endosome membrane / phagocytic vesicle membrane / peptide antigen binding / early endosome membrane / immune response ...antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / lumenal side of endoplasmic reticulum membrane / ER to Golgi transport vesicle membrane / positive regulation of T cell mediated cytotoxicity / recycling endosome membrane / phagocytic vesicle membrane / peptide antigen binding / early endosome membrane / immune response / external side of plasma membrane / signaling receptor binding / extracellular space / metal ion binding 類似検索 - 分子機能
MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type ...MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold 類似検索 - ドメイン・相同性
ジャーナル: Nat Commun / 年: 2023 タイトル: Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEM. 著者: Kei Saotome / Drew Dudgeon / Kiersten Colotti / Michael J Moore / Jennifer Jones / Yi Zhou / Ashique Rafique / George D Yancopoulos / Andrew J Murphy / John C Lin / William C Olson / Matthew C Franklin / 要旨: The recognition of antigenic peptide-MHC (pMHC) molecules by T-cell receptors (TCR) initiates the T-cell mediated immune response. Structural characterization is key for understanding the specificity ...The recognition of antigenic peptide-MHC (pMHC) molecules by T-cell receptors (TCR) initiates the T-cell mediated immune response. Structural characterization is key for understanding the specificity of TCR-pMHC interactions and informing the development of therapeutics. Despite the rapid rise of single particle cryoelectron microscopy (cryoEM), x-ray crystallography has remained the preferred method for structure determination of TCR-pMHC complexes. Here, we report cryoEM structures of two distinct full-length α/β TCR-CD3 complexes bound to their pMHC ligand, the cancer-testis antigen HLA-A2/MAGEA4 (230-239). We also determined cryoEM structures of pMHCs containing MAGEA4 (230-239) peptide and the closely related MAGEA8 (232-241) peptide in the absence of TCR, which provided a structural explanation for the MAGEA4 preference displayed by the TCRs. These findings provide insights into the TCR recognition of a clinically relevant cancer antigen and demonstrate the utility of cryoEM for high-resolution structural analysis of TCR-pMHC interactions.
全体 : Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microg...
全体
名称: Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microglobulin, MAGE-A4 peptide in complex with anti-Beta-2-microglobulin Fab 2M2
要素
複合体: Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microglobulin, MAGE-A4 peptide in complex with anti-Beta-2-microglobulin Fab 2M2
タンパク質・ペプチド: Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera
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超分子 #1: Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microg...
超分子
名称: Single chain disulfide stabilized trimer of HLA-A2, Beta-2-microglobulin, MAGE-A4 peptide in complex with anti-Beta-2-microglobulin Fab 2M2 タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all
由来(天然)
生物種: Homo sapiens (ヒト)
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分子 #1: Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera
分子
名称: Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera タイプ: protein_or_peptide / ID: 1 / コピー数: 3 / 光学異性体: LEVO