Of immunoglobulins

Chothia C, A M Lesk, A Tramontano, M Levitt, S Smith-Gill, G Air, S Sheriff, E A Padlan and D Davies 1989. Conformations of Immunoglobulin Hypervariable Regions. Nature 342 877-883. 

C Chothia, AM Lesk. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 196 901-917, 1987. 

C Chothia, AM Lesk, M Levitt, AG Amit, RA Mariuzza, SEV Phillips, RJ Poljak. The predicted structure of immunoglobulin dl.3 and its comparison with the crystal stracture. Science 233 755-758, 1986. 

In this chapter we will discuss immunoglobulins of the IgG class, which is the major type of immunoglobulin in normal human serum, and which has the simplest structure. Each chain of an IgG molecule is divided into domains of about 110 amino acid residues. The light chains have two such domains, and the heavy chains have four. 

Figure 1S.6 Enzymatic cleavage of immunoglobulin IgG. The enzyme papain splits the molecule in the hinge region, yielding two Fab fragments and one Fc fragment.

Figure IS. 7 The constant domains of immunoglobulins are folded into a compressed antiparallel p banel built up from one three-stranded p sheet packed against a four-stranded sheet (a). A topological diagram (b) shows the connected Greek key motifs of this fold.

Chothia, C., et al. Conformations of immunoglobulin hypervariable regions. Nature 343 877-883, 1989. 

Kast, E., Pathmanbhan, N., Wong, J., O Connor, B., and Klein, M. (1996). Poster presented at Protein Society 1996, Preparative Isolation of Immunoglobulin Heavy and Light Chains by Size-Exclusion Chromatogtaphy . 

FIGURE 1.11 Three -dimensional spacefilling representation of part of a protein molecule, the antigen-binding domain of immunoglobulin G (IgG). Immunoglobulin G is a major type of circulating antibody. Each of the spheres represents an atom in the structure. 

T. K. Nadler, S. K. Paliwal and F. E. Regnier, Rapid, automated, two-dimensional liigh-performance liquid cliromatographic analysis of immunoglobulin G and its multimers , 7. Chromatogr. A 676 331-335 (1994). 

Type I allergic reactions are inappropriate immune responses to an allergen with preferential synthesis of immunoglobulin E (IgE), a special antibody class, which binds to mast cells and basophilic granulocytes via Fee receptors. Binding of the allergen to the cell-bound IgE initiates the rapid release of allergic mediators, most prominently histamine, and the de novo synthesis of arachidonic acid metabolites and cytokines, which are responsible for the clinical symptoms. 

Finbloom DS, Metzger H Binding of immunoglobulin E to the receptor on rat peritoneal macrophages. J Immunol 1982 129 2004-2008. 

Bansal G, Xie Z, Rao S, Nocka KH, Druey KM Sup- 54 pression of immunoglobulin E-mediated allergic responses by regulator of G protein signaling 13. 

The repair of double-strand breaks is part of the physiologic process of immunoglobulin gene rearrangement. It... 

Five classes of H chain have been found in humans (Table 50-7), distinguished by differences in their Cjl regions. They are designated y, a, i 5, and e. The i and e chains each have four domains rather than the usual three. The type of H chain determines the class of immunoglobulin and thus its effector function. There are thus five immunoglobulin classes IgG, IgA, IgM, IgD, and IgE. The biologic functions of these five classes are summarized in Table 50-8. 

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