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T cells

TCR docking

Nature Reviews Immunology volume 2, page 626 (2002)Cite this article

The TCR molecule is a dimer composed of an α- and a β-chain, each of which consists of constant and variable immunoglobulin-like domains. The regions within the variable domains that comprise the peptide–MHC-binding interface are known as the complementarity-determining regions (CDRs). CDR1 and CDR2 seem to be positioned over the MHC molecule, whereas CDR3 seems to be positioned over the peptide.

Using the well-characterized TCR 2B4, which interacts with the moth cytochrome C (MCC)–IEk peptide–MHC complex, Wu and colleagues analysed the contribution of individual residues in the MCC–IEk complex to TCR binding by alanine-scanning mutagenesis and assessed binding affinity using surface plasmon resonance. Mutagenesis of the TCR-contact residues in MCC markedly disrupted binding, which indicates that peptide residues are important for the stable interaction of TCR and peptide–MHC.

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ORIGINAL RESEARCH PAPER

  1. Wu, L. C., Tuot, D. S., Lyons, D. S., Garcia, K. C. & Davis, M. M. Two-step binding mechanism for T-cell receptor recognition of peptide–MHC. Nature 418, 552–556 (2002)

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  1. Elaine Bell
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Bell, E. TCR docking. Nat Rev Immunol 2, 626 (2002). https://doi.org/10.1038/nri898

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  • DOI: https://doi.org/10.1038/nri898

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