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The crystal structure of a recombinant mouse single chain CD8αβ ectodomains at 2.4 Å resolution reveals paired immunoglobulin variable region-like domains with a striking resemblance to CD8αα in size, shape, and surface electrostatic potential of complementarity-determining regions (CDR), despite <20% sequence identity between the CD8α and CD8β subunits. Unlike the CD8α subunit(s) in the heterodimer...
TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes...
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....
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