Structure of class I proteins

The K/D/L proteins are trimers consisting of f}2-microglobulin, which is invariant, a polymorphic heavy chain and a highly variable peptide. The 45 kDa polymorphic K/D/L heavy chain is further divided into specific domains. The al and a2 domains each donate a helix and four strands of anti-paraJlel 3 sheet. These combine to form a cleft with two a helices running along the edges, a (3 sheet as the floor and the peptide bound in the middle, like a hot dog in a bun. This structure is quite robust. Al) the class I protein structures are very similar. The overall structure is independent of the allele or peptide bound. While the primary amino acid sequences of different class I molecules can differ by up to 30%, and they have completely unrelated peptides bound, the a carbon backbones are nearly identical. Surprisingly, the peptide, which provides much of the specificity of interaction with CDS T cells, is largely buried in the structure with only a few atoms directly accessible to the T cell receptor.

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