Paper Citing VMD - Abstract
Tynan, F.E., Reid, H.H., Kjer-Nielsen, L., Miles, J.J., Wilce, M.C.J., 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
NATURE IMMUNOLOGY, 8:268-276, MAR 2007
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.