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T Cell Receptor-MHC Class I Peptide Interactions : Affinity, Kinetics, and Specificity
Corr, Maripat,Slanetz, Alfred E.,Boyd, Lisa F.,Jelonek, Marie T.,Khilko, Sergei,Al-Ramadi, Basel K.,Kim, Young Sang,Maher, Stephen E.,Bothwell, Alfred L. M.,Margulies, David H. 충남대학교 생물공학연구소 1996 생물공학연구지 Vol.4 No.-
The critical discriminatory event in the activation of T lymphocytes bearing αβT cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded classⅠor 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 classⅠ 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 (2.6×10^-2) second^-1, corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1×10^ 5 M^-1 second^-1. The equilibrium constant for dissociation was approximately 10^-7M These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.