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The T cell surface glycoprotein CD8 enhances T cell antigen recognition by binding to MHC class I molecules. We show that human CD8 alphaalpha binds to the MHC class I molecule HLA-A2 with an extremely low affinity (Kd approximately 0.2 mM at 37 degrees C) and with kinetics that are between 2 and 3 orders of magnitude faster than reported for T cell receptor/peptide-MHC interactions. Furthermore, CD8 alphaalpha had no detectable effect on a T cell receptor (TCR) binding to the same peptide-MHC class I complex. These binding properties provide an explanation as to why the CD8/MHC class I interaction is unable to initiate cell-cell adhesion and how it can enhance TCR recognition without interfering with its specificity.

Type

Journal article

Journal

Immunity

Publication Date

02/1999

Volume

10

Pages

219 - 225

Keywords

Animals, Biosensing Techniques, CD8 Antigens, Cell Adhesion, Dimerization, HLA-A2 Antigen, Humans, Kinetics, Mice, Protein Conformation, Receptors, Antigen, T-Cell