3UYR
Structure of a monoclonal antibody complexed with its MHC-I antigen
3UYR の概要
| エントリーDOI | 10.2210/pdb3uyr/pdb |
| 関連するPDBエントリー | 3UO1 3V4U 3V52 |
| 分子名称 | antibody Fab heavy chain, antibody Fab light chain, H-2 class I histocompatibility antigen, L-D alpha chain, ... (5 entities in total) |
| 機能のキーワード | ig-fold 3, 10 helix, immune system |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| 細胞内の位置 | Membrane; Single-pass type I membrane protein: P01897 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 48180.65 |
| 構造登録者 | Margulies, D.H.,Mage, M.G.,Wang, R.,Natarajan, K. (登録日: 2011-12-06, 公開日: 2012-07-25, 最終更新日: 2024-11-20) |
| 主引用文献 | Mage, M.G.,Dolan, M.A.,Wang, R.,Boyd, L.F.,Revilleza, M.J.,Robinson, H.,Natarajan, K.,Myers, N.B.,Hansen, T.H.,Margulies, D.H. The Peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics. J.Immunol., 189:1391-1399, 2012 Cited by PubMed Abstract: MHC class I (MHC-I) proteins of the adaptive immune system require antigenic peptides for maintenance of mature conformation and immune function via specific recognition by MHC-I-restricted CD8(+) T lymphocytes. New MHC-I molecules in the endoplasmic reticulum are held by chaperones in a peptide-receptive (PR) transition state pending release by tightly binding peptides. In this study, we show, by crystallographic, docking, and molecular dynamics methods, dramatic movement of a hinged unit containing a conserved 3(10) helix that flips from an exposed "open" position in the PR transition state to a "closed" position with buried hydrophobic side chains in the peptide-loaded mature molecule. Crystallography of hinged unit residues 46-53 of murine H-2L(d) MHC-I H chain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformation. Docking and molecular dynamics predict how this segment moves to help form the A and B pockets crucial for the tight peptide binding needed for stability of the mature peptide-loaded conformation, chaperone dissociation, and Ag presentation. PubMed: 22753930DOI: 10.4049/jimmunol.1200831 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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