|Title||Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution.|
|Publication Type||Journal Article|
|Year of Publication||1986|
|Authors||Amit, AG, Mariuzza, RA, Phillips, SE, Poljak, RJ|
|Date Published||1986 Aug 15|
|Keywords||Animals, Antibodies, Monoclonal, Antigen-Antibody Complex, Chickens, Egg White, Epitopes, Immunoglobulin Fab Fragments, Immunoglobulin Heavy Chains, Immunoglobulin Light Chains, Kinetics, Models, Molecular, Muramidase, Protein Conformation, X-Ray Diffraction|
The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques. No conformational changes can be observed in the tertiary structure of lysozyme compared with that determined in native crystalline forms. The quaternary structure of Fab is that of an extended conformation. The antibody combining site is a rather flat surface with protuberances and depressions formed by its amino acid side chains. The antigen-antibody interface is tightly packed, with 16 lysozyme and 17 antibody residues making close contacts. The antigen contacting residues belong to two stretches of the lysozyme polypeptide chain: residues 18 to 27 and 116 to 129. All the complementarity-determining regions and two residues outside hypervariable positions of the antibody make contact with the antigen. Most of these contacts (10 residues out of 17) are made by the heavy chain, and in particular by its third complementarity-determining region. Antigen variability and antibody specificity and affinity are discussed on the basis of the determined structure.