Structure of CD8

CD8 exists as a disulfide-linked dimer of either a and j8 chain or two a chains. The crystal structure of the N-terminal 113 amino acids of human CD8 revealed homology to immunoglobulin (Ig) variable domains with nine ยก3 strands divided into two fi sheets, one of four and the other of five strands. An Ig-like intersheet disulfide bridge from the B strand to the F strand is present in CD8a. Another disulfide bond may be formed between cysteines in the B strand and the C strand. The hinge region connecting the amino-terminal Ig-like domain to the transmembrane segment consists of 50 residues in the a chain and 30 residues in the j8 chain, both of which are likely to be glycosylated and sialylated. The level of sialyl-ation on the (3 chain hinge region varies with the activation state of the T cell and may have functional implications for CD8 (Figure 1).

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