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Science 12 August 1994:
Vol. 265. no. 5174, pp. 946 - 949
DOI: 10.1126/science.8052850

Articles

Science, Vol 265, Issue 5174, 946-949
Copyright © 1994 by American Association for the Advancement of Science


articles

T cell receptor-MHC class I peptide interactions: affinity, kinetics, and specificity

M Corr, AE Slanetz, LF Boyd, MT Jelonek, S Khilko, BK al-Ramadi, YS Kim, SE Maher, AL Bothwell, and DH Margulies

Molecular Biology Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892.

The critical discriminatory event in the activation of T lymphocytes bearing alpha beta T cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded class I or class II molecule on the surface of an antigen-presenting cell. The kinetics of binding were measured of a purified TCR to molecular complexes of a purified soluble analog of the murine MHC class I molecule H-2Ld (sH-2Ld) and a synthetic octamer peptide p2CL in a direct, real-time assay based on surface plasmon resonance. The kinetic dissociation rate of the MHC-peptide complex from the TCR was rapid (2.6 x 10(-2) second-1, corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1 x 10(5) M-1 second-1. The equilibrium constant for dissociation was approximately 10(-7) M. These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.


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