Antibody structure and the evolution of immunoglobulin V gene segments.

@article{Kirkham1994AntibodySA,
  title={Antibody structure and the evolution of immunoglobulin V gene segments.},
  author={Perry M. Kirkham and Harry W. Schroeder},
  journal={Seminars in immunology},
  year={1994},
  volume={6 6},
  pages={347-60}
}
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… CONTINUE READING