A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule

Fleur Elizabeth Tynan, Hugh Harrington Reid, Lars Kjer-Nielsen, John J Miles, Matthew Charles James Wilce, Lyudmila Kostenko, Natalie Borg, Nicholas A Williamson, Travis Clarke Beddoe, Anthony W Purcell, S R Burrows, James McCluskey, Jamie Rossjohn

Research output: Contribution to journalArticleResearchpeer-review

159 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)268 - 276
Number of pages9
JournalNature Immunology
Volume8
Issue number3
Publication statusPublished - 2007

Cite this

Tynan, Fleur Elizabeth ; Reid, Hugh Harrington ; Kjer-Nielsen, Lars ; Miles, John J ; Wilce, Matthew Charles James ; Kostenko, Lyudmila ; Borg, Natalie ; Williamson, Nicholas A ; Beddoe, Travis Clarke ; Purcell, Anthony W ; Burrows, S R ; McCluskey, James ; Rossjohn, Jamie. / A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. In: Nature Immunology. 2007 ; Vol. 8, No. 3. pp. 268 - 276.
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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.",
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A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. / Tynan, Fleur Elizabeth; Reid, Hugh Harrington; Kjer-Nielsen, Lars; Miles, John J; Wilce, Matthew Charles James; Kostenko, Lyudmila; Borg, Natalie; Williamson, Nicholas A; Beddoe, Travis Clarke; Purcell, Anthony W; Burrows, S R; McCluskey, James; Rossjohn, Jamie.

In: Nature Immunology, Vol. 8, No. 3, 2007, p. 268 - 276.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Wilce, Matthew Charles James

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AU - Borg, Natalie

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AU - Rossjohn, Jamie

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