6AT5
Crystal structure of HLA-B*07:02 in complex with an NY-ESO-1 peptide
Summary for 6AT5
| Entry DOI | 10.2210/pdb6at5/pdb |
| Related | 6AT6 6AVF 6AVG |
| Descriptor | HLA class I histocompatibility antigen, B-7 alpha chain, Beta-2-microglobulin, Cancer/testis antigen 1 peptide, ... (4 entities in total) |
| Functional Keywords | human leukocyte antigen, major histocompatibility complex, immune system |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Membrane; Single-pass type I membrane protein: P01889 Secreted . Note=(Microbial infection) In the presence of M: P61769 Cytoplasm : P78358 |
| Total number of polymer chains | 3 |
| Total formula weight | 55390.80 |
| Authors | Gully, B.S.,Rossjohn, J. (deposition date: 2017-08-27, release date: 2018-02-28, Last modification date: 2024-10-09) |
| 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 Cited by 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: 29531227DOI: 10.1038/s41467-018-03321-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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