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Immunity. 1998 Dec;9(6):817-26.

High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling.

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Department of Pathology and Center for Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.


We have examined binding characteristics for a single TCR interacting with five of its different peptide/MHC ligands using surface plasmon resonance. We find that very small structural changes produce ligands with similar equilibrium binding affinities (K(D)) for the TCR, but vastly different potencies for T cell activation. Ligands with similar K(D)s induce similar amounts of total phospho-zeta but distinct patterns of zeta phosphorylation. Lower potency ligands induce only incomplete phosphorylation of TCR zeta and generally have faster off-rates. Therefore, the potency of TCR ligands is primarily determined by the half-life of the TCR-ligand complex and the consequent ability to induce complete phosphorylation of zeta.

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