2OI9
Structure of the 2C/Ld/QL9 allogeneic complex
2OI9 の概要
エントリーDOI | 10.2210/pdb2oi9/pdb |
関連するPDBエントリー | 2E7L |
分子名称 | Major Histocompatibility Complex protein, T cell receptor alpha chain, T cell receptor beta chain, ... (5 entities in total) |
機能のキーワード | tcr, mhc, 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: P01897 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 47760.69 |
構造登録者 | |
主引用文献 | Colf, L.A.,Bankovich, A.J.,Hanick, N.A.,Bowerman, N.A.,Jones, L.L.,Kranz, D.M.,Garcia, K.C. How a single T cell receptor recognizes both self and foreign MHC. Cell(Cambridge,Mass.), 129:135-146, 2007 Cited by PubMed Abstract: alphabeta T cell receptors (TCRs) can crossreact with both self- and foreign- major histocompatibility complex (MHC) proteins in an enigmatic phenomenon termed alloreactivity. Here we present the 2.35 A structure of the 2C TCR complexed with its foreign ligand H-2L(d)-QL9. Surprisingly, we find that this TCR utilizes a different strategy to engage the foreign pMHC in comparison to the manner in which it recognizes a self ligand H-2K(b)-dEV8. 2C engages both shared and polymorphic residues on L(d) and K(b), as well as the unrelated QL9 and dEV8 peptide antigens, in unique pair-wise contacts, resulting in greater structural complementarity with the L(d)-QL9 complex. In the structure of an engineered, high-affinity 2C TCR variant bound to H-2L(d)-QL9, the "wild-type" TCR-MHC binding orientation persists despite modified TCR-CDR3alpha interactions with peptide. Thus, a single TCR recognizes two globally similar, but distinct ligands by divergent mechanisms, indicating that receptor-ligand crossreactivity can occur in the absence of molecular mimicry. PubMed: 17418792DOI: 10.1016/j.cell.2007.01.048 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.35 Å) |
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