Structural basis for the specificity of antibody–antigen reactions and structural mechanisms for the diversification of antigen-binding specificities
- 1 February 1977
- journal article
- review article
- Published by Cambridge University Press (CUP) in Quarterly Reviews of Biophysics
- Vol. 10 (1), 35-65
- https://doi.org/10.1017/s0033583500000135
Abstract
The ability of an organism to cope with foreign substances (antigens) depends in part on its capacity to synthesize antibodies (immunoglobulins) of the proper binding specificity to recognize and combine with these antigens. In view of the great variety of possible antigens, antibodies, or more specifically their combining sites, display considerable variation and possess structural properties such as to enable them to bind the antigenic determinants. A vast amount of immunoglobulin sequence data has become available and the three-dimensional structures of a number of immunoglobulin fragments have been elucidated. With these results we can now begin to understand the structural aspects of antibody–antigen reactions. The crystallographic results and the sequence data have been reviewed elsewhere (Capra & Kehoe, 1975; Davies, Padlan & Segal 1975a, b; Gally, 1973; Kabat, 1976; Nisonoff, Hopper & Spring, 1975; Poljak, 1975a, b). Here, an attempt is made to interpret these structural data in terms of the structural evolution of the antibody combining site and the structural basis for the specificity of the binding of antibody to antigen. First, the pertinent crystallographic and sequence data will be presented. Next, the structural studies which reveal the complementarity between antibody and ligand will be described. Then, structural mechanisms by which different combining site structures could be generated will be reviewed.Keywords
This publication has 55 references indexed in Scilit:
- Structural basis for the specificity of phosphorylcholine-binding immunoglobulinsImmunochemistry, 1976
- Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolutionJournal of Molecular Biology, 1976
- Developmentally regulated proteins of the plasma membrane of Dictyostelium discoideum. The carbohydrate-binding proteinJournal of Molecular Biology, 1976
- Different degrees of interspecies homology in immunoglobulin λ chain constant domain correlated with three-dimensional structureNature, 1975
- Rotational allomerism and divergent evolution of domains in immunoglobulin light chainsBiochemistry, 1975
- Three-dimensional structure, function and genetic control of immunoglobulinsNature, 1975
- Primary structure of the Mcg λ chainBiochemistry, 1974
- Crystal and Molecular Structure of a Dimer Composed of the Variable Portions of the Bence-Jones Protein REIEuropean Journal of Biochemistry, 1974
- Immunoglobulin Structure: Amino Terminal Sequences of Mouse Myeloma Proteins That Bind PhosphorylcholineScience, 1974
- Specificity for phosphorylchloine of six murine myeloma proteins reactive with Pneumococcus C polysaccharide and β-lipoproteinBiochemistry, 1971