title: The association of heavy and light chain variable domains in antibodies: implications for antigen specificity.
abstract: The antigen-binding site of immunoglobulins is formed by six regions, three from the light and three from the heavy chain variable domains, which, on association of the two chains, form the conventional antigen-binding site of the antibody. The mode of interaction between the heavy and light chain variable domains affects the relative position of the antigen-binding loops and therefore has an effect on the overall conformation of the binding site. In this article, we analyze the structure of the interface between the heavy and light chain variable domains and show that there are essentially two different modes for their interaction that can be identified by the presence of key amino acids in specific positions of the antibody sequences. We also show that the different packing modes are related to the type of recognized antigen.
authors.affiliation: Department of Physics, Sapienza University of Rome, Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: Chailyan
authors.forename: Paolo
authors.initials: P
authors.lastname: Marcatili
authors.forename: Anna
authors.initials: A
authors.lastname: Tramontano
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry; D000918:Antibody Specificity / Q000276:immunology; D001666:Binding Sites, Antibody / Q000276:immunology; D006801:Humans; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry* / Q000276:immunology; D007147:Immunoglobulin Light Chains / Q000276:immunology
chemical_list: D000906:Antibodies; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains