期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：1
页码：504-508
DOI：10.1073/pnas.78.1.504
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
