Abstract
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 language | English (US) |
---|---|
Pages (from-to) | 946-949 |
Number of pages | 4 |
Journal | Science |
Volume | 265 |
Issue number | 5174 |
DOIs | |
State | Published - Aug 12 1994 |
Externally published | Yes |
ASJC Scopus subject areas
- General