7JWI

Crystal structure of B17.R2 TCR in complex with H2D-b-NP366

7JWI の概要

• エントリーDOI: 10.2210/pdb7jwi/pdb
• 分子名称: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, Nucleoprotein, ... (7 entities in total)
• 機能のキーワード: tcr, mhc, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 104838.18

構造登録者

Farenc, C.,Rossjohn, J. (登録日: 2020-08-25, 公開日: 2021-07-07, 最終更新日: 2024-10-09)

主引用文献

Zareie, P.,Szeto, C.,Farenc, C.,Gunasinghe, S.D.,Kolawole, E.M.,Nguyen, A.,Blyth, C.,Sng, X.Y.X.,Li, J.,Jones, C.M.,Fulcher, A.J.,Jacobs, J.R.,Wei, Q.,Wojciech, L.,Petersen, J.,Gascoigne, N.R.J.,Evavold, B.D.,Gaus, K.,Gras, S.,Rossjohn, J.,La Gruta, N.L.
Canonical T cell receptor docking on peptide-MHC is essential for T cell signaling.
Science, 372:-, 2021

PubMed Abstract: T cell receptor (TCR) recognition of peptide-major histocompatibility complexes (pMHCs) is characterized by a highly conserved docking polarity. Whether this polarity is driven by recognition or signaling constraints remains unclear. Using "reversed-docking" TCRβ-variable (TRBV) 17 TCRs from the naïve mouse CD8 T cell repertoire that recognizes the H-2D-NP epitope, we demonstrate that their inability to support T cell activation and in vivo recruitment is a direct consequence of reversed docking polarity and not TCR-pMHCI binding or clustering characteristics. Canonical TCR-pMHCI docking optimally localizes CD8/Lck to the CD3 complex, which is prevented by reversed TCR-pMHCI polarity. The requirement for canonical docking was circumvented by dissociating Lck from CD8. Thus, the consensus TCR-pMHC docking topology is mandated by T cell signaling constraints.

PubMed: 34083463
DOI: 10.1126/science.abe9124

実験手法

X-RAY DIFFRACTION (3.02 Å)