T Cell Receptor-MHC Class I Peptide Interactions: Affinity, Kinetics, and Specificity

Citations Over TimeTop 1% of 1995 papers

Abstract

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.

Related Papers

• → T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex(2011)261 cited
• → Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability(2010)114 cited
• → Current status and future challenges in T-cell receptor/peptide/MHC molecular dynamics simulations(2015)56 cited
• → Molecular modeling of a T-cell receptor bound to a major histocompatibility complex molecule: Implications for T-cell recognition(1995)12 cited
• → Engagement of a T cell receptor by major histocompatibility complex irrespective of peptide(1997)7 cited