Primary structure of the Fc region of human immunoglobulin D: implications for evolutionary origin and biological function.


We have determined the complete amino acid sequence of a tryptic Fc delta fragment generated from an intact human IgD (WAH); it is 226 residues long and includes the second (C delta 2) and the third (C delta 3) constant domains of the delta chain. Comparison of the homology of the Fc sequence of the five human immunoglobulin classes suggests that either the delta-chain gene evolved from the alpha-chain gene soon after the divergence of a mu-alpha common ancestor or it evolved from an ancestral gene distinct from both the mu-alpha and the gamma-epsilon common ancestors. Comparative study using a spatial model of the Fc region indicates that the structure of the C delta 3 domain differs extensively from that of the carboxy-terminal domains of other heavy chain classes; this, together with the unique hinge region structure, probably reflects the biological role of IgD as a receptor molecule on the B-lymphocyte surface.

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