Structural conservation of hypervariable regions in immunoglobulins evolution

Nat Struct Biol. 1994 Dec;1(12):915-20. doi: 10.1038/nsb1294-915.

Abstract

Analysis of human and mouse immunoglobulins has shown that five of six hypervariable regions that form the antigen binding site have a small repertoire of main chain conformations (canonical structures). Cartilaginous fishes are the most distantly related species to humans known to have an immune system, their evolutionary lines having diverged 450 million years ago. An analysis of VH and V kappa sequences from these fishes shows that all the main chain structures in their L1, L2, H1 and H2 hypervariable regions, and one of those in the L3 region, are the same as those most commonly found in human and mouse. This implies that the canonical structures occurring most commonly in hypervariable regions arose very early in the stages of the evolution of the immune system.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites, Antibody / genetics
  • Biological Evolution*
  • Conserved Sequence
  • Humans
  • Immunoglobulin Heavy Chains / chemistry
  • Immunoglobulin Heavy Chains / genetics
  • Immunoglobulin Variable Region / chemistry*
  • Immunoglobulin Variable Region / genetics*
  • Immunoglobulin kappa-Chains / chemistry
  • Immunoglobulin kappa-Chains / genetics
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Sequence Homology, Amino Acid
  • Sharks / genetics
  • Sharks / immunology
  • Skates, Fish / genetics
  • Skates, Fish / immunology
  • Species Specificity

Substances

  • Immunoglobulin Heavy Chains
  • Immunoglobulin Variable Region
  • Immunoglobulin kappa-Chains

Associated data

  • GENBANK/U15014
  • GENBANK/U15043
  • GENBANK/U15141
  • GENBANK/U15142
  • GENBANK/U15144
  • GENBANK/U15145