5SWS

Crystal Structure of NP2-B17 TCR-H2Db-NP complex

5SWS の概要

• エントリーDOI: 10.2210/pdb5sws/pdb
• 関連するPDBエントリー: 5SWZ
• 分子名称: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, influenza NP366 epitope, ... (6 entities in total)
• 機能のキーワード: h2db, influenza, np366, reversed docking, naive t cell, np1-b17 tcr, tcr, t cell, 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: P01899; Secreted: P01887
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 95950.00

構造登録者

Gras, S.,Del Campo, C.M.,Farenc, C.,Josephs, T.M.,Rossjohn, J. (登録日: 2016-08-08, 公開日: 2016-10-05, 最終更新日: 2024-11-13)

主引用文献

Gras, S.,Chadderton, J.,Del Campo, C.M.,Farenc, C.,Wiede, F.,Josephs, T.M.,Sng, X.Y.,Mirams, M.,Watson, K.A.,Tiganis, T.,Quinn, K.M.,Rossjohn, J.,La Gruta, N.L.
Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response.
Immunity, 45:749-760, 2016

PubMed Abstract: The anti-viral T cell response is drawn from the naive T cell repertoire. During influenza infection, the CD8 T cell response to an H-2D-restricted nucleoprotein epitope (NP) is characterized by preferential expansion of T cells bearing TRBV13 T cell receptors (TCRs) and avoidance of TRBV17 T cells, despite the latter dominating the naive precursor repertoire. We found two TRBV17 TCRs that bound H-2D-NP with a 180° reversed polarity compared to the canonical TCR-pMHC-I docking. The TRBV17 β-chain dominated the interaction and, whereas the complementarity determining region-3 (CDR3) loops exclusively mediated contacts with the MHC-I, peptide specificity was attributable to germline-encoded recognition. Nevertheless, the TRBV17 TCR exhibited moderate affinity toward H-2D-NP and was capable of signal transduction. Thus, the naive CD8 T cell pool can comprise TCRs adopting reversed pMHC-I docking modes that limit their involvement in the immune response.

PubMed: 27717799
DOI: 10.1016/j.immuni.2016.09.007

実験手法

X-RAY DIFFRACTION (2.86 Å)