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

Maripat Corr, Alfred E. Slanetz, Lisa F. Boyd, Marie T. Jelonek, Sergei Khilko, Basel K. Al-Ramadi, Young Sang Kim, Stephen E. Maher, Alfred L.M. Bothwell, David H. Margulies

Research output: Contribution to journalArticlepeer-review

311 Citations (Scopus)


The critical discriminatory event in the activation of T lymphocytes bearing αβ 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-2L(d) (sH-2L(d)) 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 105 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.

Original languageEnglish
Pages (from-to)946-949
Number of pages4
Issue number5174
Publication statusPublished - Aug 12 1994
Externally publishedYes

ASJC Scopus subject areas

  • General


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