Antibody structure and the evolution of immunoglobulin v gene segments

Academic Article

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 pnmarily 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. © 1994 Academic Press. All rights reserved.
  • Published In

    Digital Object Identifier (doi)

    Author List

  • Kirkham PM; Schroeder HW
  • Start Page

  • 347
  • End Page

  • 360
  • Volume

  • 6
  • Issue

  • 6