2NX5
Crystal structure of ELS4 TCR bound to HLA-B*3501 presenting EBV peptide EPLPQGQLTAY at 1.7A
Summary for 2NX5
Entry DOI | 10.2210/pdb2nx5/pdb |
Descriptor | HLA-B35, Beta-2-microglobulin, EBV peptide, EPLPQGQLTAY, ... (6 entities in total) |
Functional Keywords | tcr-pmhc, immune complex, immune system |
Biological source | Homo sapiens (human) More |
Cellular location | Secreted: P61769 |
Total number of polymer chains | 20 |
Total formula weight | 372980.36 |
Authors | Tynan, F.E.,Reid, H.H.,Rossjohn, J. (deposition date: 2006-11-16, release date: 2007-02-27, Last modification date: 2023-10-25) |
Primary citation | Tynan, F.E.,Reid, H.H.,Kjer-Nielsen, L.,Miles, J.J.,Wilce, M.C.,Kostenko, L.,Borg, N.A.,Williamson, N.A.,Beddoe, T.,Purcell, A.W.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule Nat.Immunol., 8:268-276, 2007 Cited by PubMed Abstract: Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide. PubMed: 17259989DOI: 10.1038/ni1432 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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