Constant domains structure

The overall structure of the variable domain is very similar to that of the constant domain, hut there are nine p strands instead of seven. The two additional p strands are inserted into the loop region that connects p strands C and D (red in Figure 15.8). Functionally, this part of the polypeptide chain is important since it contains the hypervariahle region CDR2. The two extra p strands, called C and C", provide the framework that positions CDR2 close to the other two hypervariahle regions in the domain structure (Figure 15.8). 

IgG antibody molecules are composed of two light chains and two heavy chains joined together by disulfide bonds. Each light chain has one variable domain and one constant domain, while each heavy chain has one variable and three constant domains. All of the domains have a similar three-dimensional structure known as the immunoglobulin fold. The Fc stem of the molecule is formed by constant domains from each of the heavy chains, while two Fab arms are formed by constant and variable domains from both heavy and light chains. The hinge region between the stem and the arms is flexible and allows the arms to move relative to each other and to the stem. 

The constant domain has a stable framework structure composed of two antiparallel sheets comprising seven p strands, four in one sheet and three in the other. The variable domains have a similar framework structure but comprising nine p strands, five in one sheet and four in the other. The three hypervariable regions are in loops at one end of the variable domain. The variable domains from the heavy and light chains associate through their five-stranded p sheets to form a barrel with the hypervariable loop regions from both domains close together at the top of the barrel. 

Figure 1.10. Generalised structure of the variable and constant domains within antibodies. The variable regions (dark shading) of either the light or heavy chains are indicated as VL or VH, respectively. The light chains also possess one constant region (CL), whereas the heavy chains possess either three or four constant regions (Ch)-Ch4). depending upon the class of immunoglobulin (see text for details).

The fundamental structure of immunoglobulins was first established by Gerald Edelman and Rodney Porter. Each chain is made up of identifiable domains some are constant in sequence and structure from one IgG to the next, others are variable. The constant domains have a characteristic structure known as the immunoglobulin fold, a well-conserved structural motif in the all /3 class of proteins (Chapter 4). There are three of these constant domains in each heavy chain and one in each light chain. The heavy and light chains also have one variable domain each, in which most of the variability in amino acid residue sequence is found. The variable domains associate to create the antigen-binding site (Fig. 5-24). 

Here n is the average refractive index, k is Boltzman s constant, and T is absolute temperature (13). If a polyblend were to form a homogeneous network, the stress would be distributed equally between network chains of different composition. Assuming that the size of the statistical segments of the component polymers remains unaffected by the mixing process, the stress-optical coefficient would simply be additive by composition. Since the stress-optical coefficient of butadiene-styrene copolymers, at constant vinyl content, is a linear function of composition (Figure 9), a homogeneous blend of such polymers would be expected to exhibit the same stress-optical coefficient as a copolymer of the same styrene content. Actually, all blends examined show an elevation of Ka which increases with the breadth of the composition distribution (Table III). Such an elevation can be justified if the blends have a two- or multiphase domain structure in which the phases differ in modulus. If we consider the domains to be coupled either in series or in parallel (the true situation will be intermediate), then it is easily shown that... 

FIGURE 22.1 Pentameric structure of IgM IgM is composed of a pentamer of the basic four chain structure held together by inter H chain disulfide bonds. The heavy chain (p) has four constant domains. A small, cysteine rich protein called J chain initiates cross linking of C3 and C4 of five IgM monomers to make the circulating, pentameric form of IgM. 

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