Fig. 4.5 the structure of immunoglobulin constant and variable domains.
The upper panels show schematically the folding pattern of the constant(C) and variable(V) domains of an immunoglobulin light chain. Each domain is a barrel-shaped structure in which strands of polypeptide chain(β strands) running in opposite directions β sheets (shown in yellow and green for the C domain and red and blue for the V domain), which and held together by a disulfide bond. The way in which the polypeptide chain folds to give the final structure can be seen more clearly when the sheets are opened out, as shown in the lower panels. The β strands are lettered sequentially with respect to the order of their occurrence in the amino acid sequence of the domains; the order in each β sheet is characteristic of immunoglobulin domains. The β strands C’ and C’’ that are found in the V domain but not in the C domains are indicated by a blue shaded background. The characteristic four-strand plus three-strand(C-region type domain) or four-strand plus five-strand(V-region type domain) arrangements are typical immunoglobulin superfamily domain building blocks, found in a whole range of other proteins as well as antibodies and T-cell receptors.