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Immunoglobulin protein (Ig), also known as antibody, is a major effector protein of the immune system. Produced by B cells, Ig has a highly conserved constant region and an antigen binding region that is hypervariable. Within this variable region, however, some amino acid sequences are more subject to variation than others. We examined this variation by constructing a sequence alignment of 9 human Ig epsilon heavy chain amino acid sequences. ConSurf was used to visualize the location of variable sites. Variation was not uniformly distributed; the greatest degree of variation was observed in the loops that extend to form part of the antigen binding site.
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