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Figure Molecules with multiple antigenic determinants. A A globular protein is shown with a of different antigenic determinants. Different regions of a polypeptide chain usually come together in the folded structure to form each antigenic determinant more The reversible binding reaction between an antigen with a single antigenic determinant denoted Ag and a single antigen- binding site denoted Ab can be expressed as The equilibrium point depends both on the concentrations of Ab and Ag and on the strength of their interaction. Clearly, a larger fraction of Ab will become associated with Ag as the concentration of Ag increases.

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Figure Molecules with multiple antigenic determinants.

A A globular protein is shown with a of different antigenic determinants. Different regions of a polypeptide chain usually come together in the folded structure to form each antigenic determinant more The reversible binding reaction between an antigen with a single antigenic determinant denoted Ag and a single antigen- binding site denoted Ab can be expressed as The equilibrium point depends both on the concentrations of Ab and Ag and on the strength of their interaction.

Clearly, a larger fraction of Ab will become associated with Ag as the concentration of Ag increases. The strength of the interaction is generally expressed as the affinity constant K a see Figurewhere the square brackets indicate the concentration of each component at equilibrium.

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The affinity constant, sometimes called the association constantcan be determined by measuring the concentration of free Ag required to fill half of the antigen -binding sites on the antibody. Thus, the reciprocal of the antigen concentration that produces half the maximum binding is equal to the affinity constant of the antibody for the antigen. The affinity of an antibody for an antigenic determinant describes the strength of binding of a single copy of the antigenic determinant to a single antigen - binding siteand it is independent of the of sites.

When, however, a polyvalent antigen, carrying multiple copies of the same antigenic determinant, combines with a polyvalent antibody, the binding strength is greatly increased because all of the antigen-antibody bonds must be gar,and simultaneously before the antigen and antibody can dissociate. As a result, a typical IgG molecule can bind at least times more strongly to a polyvalent antigen if both antigen-binding sites are engaged than if only one site is engaged.

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The total binding strength of a polyvalent antibody with a polyvalent antigen is referred to as the avidity of the interaction. If the affinity of the antigen -binding sites in an IgG and an IgM molecule is the same, the IgM molecule with 10 typees sites will have a much greater avidity for a multivalent antigen than an IgG molecule which has two binding sites.

This difference in avidity, often fold or more, is important because antibodies produced early in an immune response usually have much lower affinities than those produced later. Because of its high total avidity, IgM—the major Ig class produced early in immune responses—can function effectively even when each of its binding sites has only a low affinity. So far we have considered the general structure and function of antibodies.

Next we look at the details of their structure, as revealed by studies of their amino acid sequence and three-dimensional structure. Light and Heavy Chains Consist of Constant and Variable Regions Comparison of the amino acid sequences of different antibody molecules reveals a striking feature with important genetic implications. Both light and heavy chains have a gypes sequence at their N-terminal ends but a constant sequence at their C-terminal ends.

Light chains have a constant region about amino acids long and a variable region of the same size. The variable region of the heavy chains at their N-terminus is also about amino acids long, but the heavy-chain constant region is about three or four times longer or amino acidsdepending on the class Figure Figure Constant and variable regions of immunoglobulin chains.

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Both light and heavy chains of an antibody molecule have distinct constant and variable regions. It is the N-terminal ends of the light and heavy chains that come together to form the antigen - binding site see Figureand the variability of their amino acid sequences provides the structural basis for the diversity of antigen-binding sites.

The diversity in the variable regions of both light and heavy type is for the most part restricted to three small hypervariable regions in each chain; the remaining parts of the variable regionknown as framework regions, are relatively constant. Only the 5—10 amino acids in each hypervariable region form the antigen-binding site Figure Vreat a result, the size of the antigenic determinant that an antibody recognizes is generally comparably small.

It can consist of fewer than 25 amino acids on the surface of a globular proteinfor example. Antibody hypervariable regions. Highly schematized drawing of how the three hypervariable regions in each light and heavy chain together form the antigen-binding site of an antibody molecule.

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The Light and Heavy Chains Are Composed of Repeating Ig Domains Both light and heavy chains are made up of repeating segments—each about amino acids long and each containing one intrachain disulfide bond. These repeating segments fold independently to form compact functional units called immunoglobulin Ig domains.

As shown in Figurea light chain consists of one variable VL and one constant CL domain equivalent to the variable and constant regions shown in the top half of Figure These domains pair with the variable VH and first constant CH1 domain of the heavy chain to form the antigen -binding region. The remaining constant domains of the heavy chains form the Fc region, typds determines the sb biological properties of the antibody.

Figure Immunoglobulin domains. The light and heavy chains in an antibody molecule are each folded into repeating domains that are similar to one another.

The variable domains shaded in blue of the light and heavy chains VL and VH make up the antigen-binding more The similarity in their domains suggests that antibody chains arose during evolution by a series of gene duplications, beginning with a primordial gene coding for a single amino acid domain of unknown function. This hypothesis is supported by the finding that each domain of the constant region of a heavy chain is encoded by a separate coding sequence exon Figure Figure The organization of the DNA sequences that encode the constant region of an antibody heavy chain.

The coding sequences exons for each domain and for the hinge region are separated by noncoding sequences introns. The intron sequences are removed by more An Antigen-Binding Site Is Constructed From Hypervariable Loops A of fragments of antibodies, as well as intact antibody molecules, have been studied by x-ray crystallography. From these examples, we can understand the way in which billions of different antigen -binding sites are constructed on a common structural theme.

We shall see later that many other proteins on the surface of lymphocytes and other cells, many of which function as cell-cell adhesion molecules discussed in Chapter 19contain similar domains and hence are members of a very large immunoglobulin Ig superfamily of proteins. Figure The folded structure of an IgG antibody molecule, based on x-ray crystallography studies. The structure of the whole protein is shown in the middle, while the structure of a constant domain is shown on the left and of a variable domain on the right.

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Both more The variable domains of antibody molecules are unique in that each has its particular set of three hypervariable regions, which are arranged in three hypervariable loops see Figure The hypervariable loops of both the light and heavy variable domains are clustered together to form the antigen - binding site. Because the variable region of an antibody molecule consists of a highly conserved rigid framework, with hypervariable loops attached at one end, an enormous diversity of antigen-binding sites can be generated by changing only the lengths and amino acid sequences of the hypervariable loops.

The overall three-dimensional structure necessary for antibody function remains constant. X-ray analyses of crystals of antibody fragments bound to an antigenic determinant reveal exactly how the hypervariable loops of the light and heavy variable domains cooperate to form an antigen -binding surface in particular cases.

The dimensions and shape of each different site vary depending on the conformations of the polypeptide chain in the hypervariable loops, which in turn are determined by the sequences of the amino acid side chains in the loops. The shapes of binding sites vary greatly—from pockets, to grooves, to undulating flatter surfaces, and even to protrusions—depending on the antibody Figure Smaller ligands tend to bind to deeper pockets, whereas larger seekiing tend to bind to flatter surfaces.

In addition, the binding site can alter its shape after antigen q to better fit the ligand.

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Figure Antigen-binding sites of antibodies. The hypervariable loops of different VL and VH domains can combine to form a large variety of binding surfaces. The antigenic determinants and the antigen-binding site of the antibodies are shown in red.

Only one antigen-binding more Now that we have discussed the structure and functions of antibodies, we are ready to consider the crucial question that puzzled immunologists for many years—what are the genetic mechanisms that enable each of us to make many billions of different antibody molecules? Summary Antibodies defend vertebrates against infection by inactivating viruses and microbial toxins and by recruiting the complement system and various types of white blood cell to kill the invading pathogens.

Each B cell clone makes antibody molecules with a unique antigen - binding site. Initially, during B cell development in the bone marrow, the antibody molecules are inserted into the plasma membranewhere they serve as receptors for antigen. In peripheral lymphoid organs, antigen binding to these receptors, together with costimulatory als provided by helper T cells, activates the B cells to proliferate and differentiate into either memory cells or antibody-secreting effector cells.

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The effector cells secrete antibodies with the same unique antigen-binding site as the membrane-bound antibodies. A typical antibody molecule is composed of four polypeptide chains, two identical heavy chains and two identical light chains. Parts of both the heavy and light chains usually combine to form the grland -binding sites. The heavy chains also form the tail Fc region of the antibody, which determines what other proteins will bind to the antibody and therefore what biological properties the antibody class has.

The amino acid sequence variation in the variable domains of both light and heavy chains is mainly confined to several small hypervariable regions, which protrude as loops at one end of the domains to form the antigen - binding site. By agreement with the publisher, this book is accessible by the search feature, but cannot be browsed.

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