Structure and Specificity of Antibody Molecules

R. J. Poljak, L. M. Amzel, B. L. Chen, R. P. Phizackerley, F. Saul

Abstract

The structure of the Fab' fragment of a human myeloma protein (IgG1 (<latex>$\lambda$</latex>) New) has been determined by X-ray crystallographic analysis to a nominal resolution of 0.2 nm. Each of the structure subunits corresponding to the variable and to the constant homology regions of the light and heavy polypeptide chains contains two irregular <latex>$\beta$</latex>-sheets which are roughly parallel to each other and surround a tightly packed interior of hydrophobic side chains. The regions of the hypervariable sequences in the light and heavy chains occur in close spatial proximity at one end of the molecule, defining the active site of IgG New. The role of these hypervariable regions in defining the size and shape of the active site of different immunoglobulins is discussed on the basis of the three-dimensional model of Fab' New. Several ligands that bind to the active centre of IgG New have been used to obtain crystalline ligand-Fab' New complexes which were investigated by difference Fourier maps. These studies are analysed in terms of the biological function and specificity of antibodies.

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