1. T Cell Receptor-MHC Class I Peptide Interactions: Affinity, Kinetics, and Specificity
- Author
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Stephen E. Maher, Alfred E. Slanetz, Marie T. Jelonek, Maripat Corr, Sergei Khilko, Alfred L. M. Bothwell, Basel K. al-Ramadi, Lisa F. Boyd, Young Sang Kim, and David H. Margulies
- Subjects
Stereochemistry ,Receptors, Antigen, T-Cell, alpha-beta ,T cell ,Molecular Sequence Data ,chemical and pharmacologic phenomena ,Peptide ,Biosensing Techniques ,Major histocompatibility complex ,Major Histocompatibility Complex ,Mice ,Antigen ,MHC class I ,medicine ,Animals ,Amino Acid Sequence ,Histocompatibility Antigen H-2D ,Receptor ,Peptide sequence ,chemistry.chemical_classification ,Multidisciplinary ,biology ,T-cell receptor ,H-2 Antigens ,Kinetics ,medicine.anatomical_structure ,Solubility ,chemistry ,biology.protein ,Oligopeptides - 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.
- Published
- 1995
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