title: Antibody structure and the evolution of immunoglobulin V gene segments.
abstract: Immunoglobulin V domains can be divided into eight unique segments, each of which plays a separate structural role in the creation of an antigen binding site. Three of these segments encode the VH/VL core and are preserved in all V domains. V family identity depends on sequence similarity in two segments which provide support for the antigen binding site. Within a family, gene segments primarily diverge in CDR1 and CDR2. H chain CDR3, flanked by H chain CDR1 and L chain CDRs 2 and 3, builds specificity at the center of the antigen binding site. These findings provide a structural context for interpreting the preferential use of V gene segments in specific immune responses.
authors.affiliation: Division of Developmental and Clinical Immunology, University of Alabama at Birmingham 35294-3300, USA.
authors.forename: P M
authors.initials: PM
authors.lastname: Kirkham
authors.forename: H W
authors.initials: HW
authors.lastname: Schroeder
mesh_terms: D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology*; D005075:Biological Evolution; D005803:Genes, Immunoglobulin; D006801:Humans; D007135:Immunoglobulin Variable Region / Q000235:genetics*
chemical_list: D007135:Immunoglobulin Variable Region