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Structural conservation of hypervariable regions in immunoglobulins evolution

Nature Structural Biology volume 1, pages 915–920 (1994)Cite this article

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 Vκ 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.

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Samantha Barré & Cyrus Chothia

  2. Cambridge Centre of Protein Engineering, Hills Road, Cambridge, CB2 2QH, UK

    Cyrus Chothia

  3. Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, FL, 33101, USA

    Andrew S. Greenberg & Martin F. Flajnik

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  1. Samantha Barré
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  4. Cyrus Chothia
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Barré, S., Greenberg, A., Flajnik, M. et al. Structural conservation of hypervariable regions in immunoglobulins evolution. Nat Struct Mol Biol 1, 915–920 (1994). https://doi.org/10.1038/nsb1294-915

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