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Abstract
The crystal structure of the two immunoglobulin variable–like domains of the murine CD8αα homodimer complexed to the class I MHC H-2K b molecule at 2.8 Å resolution shows that CD8αα binds to the protruding MHC α3 domain loop in an antibody-like manner. Comparison of mouse CD8αα/H-2K b and human CD8αα/HLA-A2 complexes reveals shared as well as species-specific recognition features. In both species, coreceptor function apparently involves the participation of CD8 dimer in a bidentate attachment to an MHC class I molecule in conjunction with a T cell receptor without discernable conformational alteration of the peptide or MHC antigen-presenting platform.
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