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

256Citations
Citations of this article
99Readers
Mendeley users who have this article in their library.

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.

Cite

CITATION STYLE

APA

Kersh, G. J., Kersh, E. N., Fremont, D. H., & Allen, P. M. (1998). High- and low-potency ligands with similar affinities for the TCR: The importance of kinetic in TCR signaling. Immunity, 9(6), 817–826. https://doi.org/10.1016/S1074-7613(00)80647-0

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free