Molecular Genetics of Immunoglobulin by F. Calabi and M.S. Neuberger (Eds.)

By F. Calabi and M.S. Neuberger (Eds.)

Our realizing of the molecular genetics of immunoglobulins has been significantly complicated by way of the applying of recombinant DNA know-how. This new quantity within the renowned sequence New complete Biochemistry comprises 8 chapters that draw jointly stories summarising the examine into immunoglobulins and the association, rearrangement and expression in their gene constitution. Molecular Genetics of Immunoglobulin can be of specific significance to these operating within the components of genetics and molecular biology, immunology, and mobile biology.

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These molecules display Fab and Fc structures similar or identical to the structures of the isolated fragments and are approximately T-shaped. They have been described as the 'structure of the antibody molecule'. However, some caution is necessary here as, for example, the hinge-deleted IgGl Dob protein, unlike the intact IgGl molecule, neither activates complement [34] nor binds to monocyte Fc receptor [35]. Unfortunately, crystal diffraction patterns of whole 1gG have been characterised by a lack of electron density associated with part of the hinge and the whole of the Fc, a phenomenon which has been related to hinge flexibility [36,37].

L l ( a ) . The Fc portion of IgM (C,3 and C,4 domains) is very similar to that of IgG, with t h c non-paired C,3 domains resembling the C J domains in having interposed N-linked, branched carbohydrate chains. The paired C,2 domains replace the hinge of IgG. There would, however, appear to be some potential for flexibility between the C,1 and C,2 domains and between C,2 and C,3. Indeed, electron micrographs of pentameric IgM [4] indicate a monomer in which the F(ab’)2 unit of Fig. l l ( a ) is rotated through 90” about its two-fold axis of symmetry (compare IgG1, Fig.

A dot indicates no residue at the position corresponding to the numbered human IgGl residue. S@ or T@ indicates 0-linked carbohydrate attachment sites. Cys-220 (IgG1. I g A l . IgA2) forms ii disulphide linkage to the light chain. Note lhat IgG3 and IgD in particular have long hinges but of different character. IgG3 has a long middle hinge and IgD a long upper hinge. IgAl also has a relatively long upper hinge. These differences may have important consequences for function. 5. Structure and function of IgM 5.

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