6AT6

Crystal structure of the KFJ5 TCR

Summary for 6AT6

• Entry DOI: 10.2210/pdb6at6/pdb
• Related: 6AT5 6AVF 6AVG
• Descriptor: T-cell receptor beta variable 28, Human nkt tcr beta chain chimera, T-cell receptor alpha variable 4, T-cell receptor, sp3.4 alpha chain chimera (3 entities in total)
• Functional Keywords: immunogolbulin, immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 51555.49

Authors

Gully, B.S.,Rossjohn, J. (deposition date: 2017-08-28, release date: 2018-02-28, Last modification date: 2024-10-16)

Primary citation

Chan, K.F.,Gully, B.S.,Gras, S.,Beringer, D.X.,Kjer-Nielsen, L.,Cebon, J.,McCluskey, J.,Chen, W.,Rossjohn, J.
Divergent T-cell receptor recognition modes of a HLA-I restricted extended tumour-associated peptide.
Nat Commun, 9:1026-1026, 2018

PubMed Abstract: Human leukocyte antigen (HLA)-I molecules generally bind short peptides (8-10 amino acids), although extended HLA-I restricted peptides (>10 amino acids) can be presented to T cells. However, the function of such extended HLA-I epitopes in tumour immunity, and how they would be recognised by T-cell receptors (TCR) remains unclear. Here we show that the structures of two distinct TCRs (TRAV4TRAJ21-TRBV28TRBJ2-3 and TRAV4 TRAJ8-TRBV9TRBJ2-1), originating from a polyclonal T-cell repertoire, bind to HLA-B*07:02, presenting a 13-amino-acid-long tumour-associated peptide, NY-ESO-1. Comparison of the structures reveals that the two TCRs differentially binds NY-ESO-1-HLA-B*07:02 complex, and induces differing extent of conformational change of the NY-ESO-1 epitope. Accordingly, polyclonal TCR usage towards an extended HLA-I restricted tumour epitope translates to differing TCR recognition modes, whereby extensive flexibility at the TCR-pHLA-I interface engenders recognition.

PubMed: 29531227
DOI: 10.1038/s41467-018-03321-w

Experimental method

X-RAY DIFFRACTION (1.417 Å)