@article{dfbf399cd0074d79bbd0718f178c9087,
title = "High- and low-potency ligands with similar affinities for the TCR: The importance of kinetic in TCR signaling",
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.",
author = "Kersh, \{Gilbert J.\} and Kersh, \{Ellen N.\} and Fremont, \{Daved H.\} and Allen, \{Paul M.\}",
note = "Funding Information: We thank John Kappler for providing reagents and expert advice on the production of soluble molecules and Robert Schreiber for providing the K3–53 monoclonal antibody. We thank A. S. Shaw for helpful comments on the manuscript and Jerri Smith for her help in preparation of the manuscript. We thank Jane Schrimpf, Steve Horvath, and Dave Donermeyer for technical assistance. G. J. K. was supported by a postdoctoral fellowship from the Cancer Research Institute. This work was supported by National Institutes of Health grant AI24157.",
year = "1998",
month = dec,
doi = "10.1016/S1074-7613(00)80647-0",
language = "English",
volume = "9",
pages = "817--826",
journal = "Immunity",
issn = "1074-7613",
number = "6",
}