4P2Q

Crystal structure of the 5cc7 TCR in complex with 5c2/I-Ek

4P2Q の概要

• エントリーDOI: 10.2210/pdb4p2q/pdb
• 関連するPDBエントリー: 4P2O 4P2R
• 分子名称: H-2 class II histocompatibility antigen, E-K alpha chain, MHC class II E-beta-k, 5c2 peptide, ... (6 entities in total)
• 機能のキーワード: t cell receptor, peptide-mhc complex, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 408871.86

構造登録者

Birnbaum, M.E.,Ozkan, E.,Garcia, K.C. (登録日: 2014-03-04, 公開日: 2014-05-21, 最終更新日: 2024-11-06)

主引用文献

Birnbaum, M.E.,Mendoza, J.L.,Sethi, D.K.,Dong, S.,Glanville, J.,Dobbins, J.,Ozkan, E.,Davis, M.M.,Wucherpfennig, K.W.,Garcia, K.C.
Deconstructing the Peptide-MHC Specificity of T Cell Recognition.
Cell, 157:1073-1087, 2014

PubMed Abstract: In order to survey a universe of major histocompatibility complex (MHC)-presented peptide antigens whose numbers greatly exceed the diversity of the T cell repertoire, T cell receptors (TCRs) are thought to be cross-reactive. However, the nature and extent of TCR cross-reactivity has not been conclusively measured experimentally. We developed a system to identify MHC-presented peptide ligands by combining TCR selection of highly diverse yeast-displayed peptide-MHC libraries with deep sequencing. Although we identified hundreds of peptides reactive with each of five different mouse and human TCRs, the selected peptides possessed TCR recognition motifs that bore a close resemblance to their known antigens. This structural conservation of the TCR interaction surface allowed us to exploit deep-sequencing information to computationally identify activating microbial and self-ligands for human autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here enables effective surveillance of diverse self and foreign antigens without necessitating degenerate recognition of nonhomologous peptides.

PubMed: 24855945
DOI: 10.1016/j.cell.2014.03.047

実験手法

X-RAY DIFFRACTION (3.3 Å)