Structural diversity of antibody catalysts.
The structural diversity of the immune response may be considerably restricted by the structure of the hapten used to elicit catalytic antibodies. The ligand-binding mode and the shapes of the binding pockets of hydrolytic antibodies induced to different transition-state analogs that contain an unsubstituted arylphosphonate group are very similar. Moreover, antibodies elicited against a single transition state analog evolve from a single germline gene or different precursors, depending on the nature of the hapten. Germline antibodies seem to adopt multiple conformations with antigen binding, together with somatic mutation stabilizing the conformation with optimum complementarity to antigen.
Golinelli-Pimpaneau
Béatrice
B
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS Bât. 34, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France. beatrice.golinelli@lebs.cnrs-gif.fr
D017151:Antibodies, Catalytic / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D004950:Esterases / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D017151:Antibodies, Catalytic; D004950:Esterases