Cancer Institute A national cancer institute
designated cancer center

Yueh-hsiu Chien

Publication Details

  • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists IMMUNITY Lyons, D. S., Lieberman, S. A., Hampl, J., BONIFACE, J. J., Chien, Y. H., Berg, L. J., DAVIS, M. M. 1996; 5 (1): 53-61

    Abstract:

    T lymphocyte activation is mediated by the interaction of specific TCR with antigenic peptides bound to MHC molecules. Single amino acid substitutions are often capable of changing the effect of a peptide from stimulatory to antagonistic. Using surface plasmon resonance, we have analyzed the interaction between a complex consisting of variants of the MCC peptide bound to a mouse class II MHC (Ek) and a specific TCR. Using both an improved direct binding method as well as a novel inhibition assay, we show that the affinities of three different antagonist peptide-Ek complexes are approximately 10-50 times lower than that of the wildtype MCC-Ek complex for the TCR, largely due to an increased off-rate. These results suggest that the biological effects of peptide antagonists and partial agonists may be largely based on kinetic parameters.

    View details for Web of Science ID A1996UZ45400006

    View details for PubMedID 8758894

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