Antibody structure and the evolution of immunoglobulin V gene segments

Semin Immunol. 1994 Dec;6(6):347-60. doi: 10.1006/smim.1994.1045.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • B-Lymphocytes / immunology*
  • Biological Evolution*
  • Genes, Immunoglobulin*
  • Humans
  • Immunoglobulin Variable Region / genetics*


  • Immunoglobulin Variable Region