Advances in Immunology, Vol. 44 by Frank J. Dixon (Editor)

By Frank J. Dixon (Editor)

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1987) and hence may be predominantly responsible for restricting cytoxic T cells to class-I-presented antigens and helper T cells to class-II-presented antigens (see Townsend, 1985). The human CD8 molecule is usually characterized as a homodimer of CY chains, unlike the CD8 of mouse, which is a heterodimer with an a and ,l3 chain (Lyt-2 and L3T4, respectively). The CD4 molecule appears to be monomeric. However, recent evidence indicates that the human CD8 molecule may also exist as a heterodimer employing a Lyt-3 (p) homolog 0.

In fact, when the CD28 and CTLA-4 sequences are compared, it is evident that they are very closely related (data not shown). The connecting sequence is particularly conserved (one stretch of 25 amino acids has 15 exact matches and 4 highly conservative substitutions). Also, all five extracellular cysteine residues are precisely conserved. It is quite possible that the CXLA-4 gene is the mouse homolog of the human CD28 antigen gene. Interestingly, the hingelike sequence in the CD28 chain is precisely deleted from the CTLA-4 chain.

1987). , 1987; Nose et a l . , 1987) share an analogous structural motif with N-CAM and MAG. The apparent adhesive properties of each molecule is mediated by N-terminal repeat units approximately 100 residues in length. The non-IgGSFCAM sequences each have three or four such repeats that are obviously the products of internal duplication, as appears to be the case for N-CAM and MAG. These repeats, as with H-type homology units, are predicted to have secondary structures dominated by six or seven alternating fl strands (data 38 TIM HUNKAPILLER AND LEROY HOOD not shown; after Chou and Fasman, 1978).

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