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

Gilbert J. Kersh, Ellen N. Kersh, Daved H. Fremont, Paul M. Allen

Research output: Contribution to journalArticlepeer-review

267 Scopus citations

Abstract

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-ζ but distinct patterns of ζ phosphorylation. Lower potency ligands induce only incomplete phosphorylation of TCR ζ 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 ζ.

Original languageEnglish
Pages (from-to)817-826
Number of pages10
JournalImmunity
Volume9
Issue number6
DOIs
StatePublished - Dec 1998

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