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T cell receptor engagement by peptide-MHC ligands induces a conformational change in the CD3 complex of thymocytes.

ABSTRACT: The T cell receptor (TCR) can recognize a variety of cognate peptide/major histocompatibility complex (pMHC) ligands and translate their affinity into distinct cellular responses. To achieve this, the nonsignaling alphabeta heterodimer communicates ligand recognition to the CD3 signaling subunits by an unknown mechanism. In thymocytes, we found that both positive- and negative-selecting pMHC ligands expose a cryptic epitope in the CD3 complex upon TCR engagement. This conformational change is induced in vivo and requires the expression of cognate MHC. We conclude that TCR engagement with a cognate pMHC ligand induces a conformational change in the CD3 complex of thymocytes and propose that this marks an initial event during thymic selection that signals the recognition of self-antigen.

SUBMITTER: Gil D

PROVIDER: S-EPMC1868566 | biostudies-literature | 2005 Feb

REPOSITORIES: biostudies-literature

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T cell receptor engagement by peptide-MHC ligands induces a conformational change in the CD3 complex of thymocytes.

Gil Diana D Schrum Adam G AG Alarcón Balbino B Palmer Ed E

The Journal of experimental medicine 20050201 4

The T cell receptor (TCR) can recognize a variety of cognate peptide/major histocompatibility complex (pMHC) ligands and translate their affinity into distinct cellular responses. To achieve this, the nonsignaling alphabeta heterodimer communicates ligand recognition to the CD3 signaling subunits by an unknown mechanism. In thymocytes, we found that both positive- and negative-selecting pMHC ligands expose a cryptic epitope in the CD3 complex upon TCR engagement. This conformational change is in ...[more]

PMID: 15728235

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