3C5Z
Crystal structure of mouse MHC class II I-Ab/3K peptide complexed with mouse TCR B3K506
3C5Z の概要
エントリーDOI | 10.2210/pdb3c5z/pdb |
関連するPDBエントリー | 1LNU 3C60 3C6L |
分子名称 | TCR B3K506 Alpha Chain, TCR B3K506 Beta Chain, H-2 class II histocompatibility antigen, A-B alpha chain, ... (5 entities in total) |
機能のキーワード | tcr-pmhc complex, glycoprotein, immune response, membrane, mhc ii, transmembrane, sugar binding protein-immune system complex, sugar binding protein/immune system |
由来する生物種 | Mus musculus (house mouse) 詳細 |
細胞内の位置 | Membrane ; Single-pass type I membrane protein : P14434 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 189918.63 |
構造登録者 | |
主引用文献 | Dai, S.,Huseby, E.S.,Rubtsova, K.,Scott-Browne, J.,Crawford, F.,Macdonald, W.A.,Marrack, P.,Kappler, J.W. Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules. Immunity, 28:324-334, 2008 Cited by PubMed Abstract: To test whether highly crossreactive alphabeta T cell receptors (TCRs) produced during limited negative selection best illustrate evolutionarily conserved interactions between TCR and major histocompatibility complex (MHC) molecules, we solved the structures of three TCRs bound to the same MHC II peptide (IAb-3K). The TCRs had similar affinities for IAb-3K but varied from noncrossreactive to extremely crossreactive with other peptides and MHCs. Crossreactivity correlated with a shrinking, increasingly hydrophobic TCR-ligand interface, involving fewer TCR amino acids. A few CDR1 and CDR2 amino acids dominated the most crossreactive TCR interface with MHC, including Vbeta8 48Y and 54E and Valpha4 29Y, arranged to impose the familiar diagonal orientation of TCR on MHC. These interactions contribute to MHC binding by other TCRs using related V regions, but not usually so dominantly. These data show that crossreactive TCRs can spotlight the evolutionarily conserved features of TCR-MHC interactions and that these interactions impose the diagonal docking of TCRs on MHC. PubMed: 18308592DOI: 10.1016/j.immuni.2008.01.008 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.55 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード