7JWI

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

Summary for 7JWI

• Entry DOI: 10.2210/pdb7jwi/pdb
• Descriptor: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, Nucleoprotein, ... (7 entities in total)
• Functional Keywords: tcr, mhc, immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 5
• Total formula weight: 104838.18

Authors

Farenc, C.,Rossjohn, J. (deposition date: 2020-08-25, release date: 2021-07-07, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.02 Å)