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Publication Detail
The importance of somatic mutations in the V(lambda) gene 2a2 in human monoclonal anti-DNA antibodies
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Article
  • Authors:
    Rahman A, Haley J, Radway-Bright E, Nagl S, Low DG, Latchman DS, Isenberg DA
  • Publication date:
    16/03/2001
  • Pagination:
    149, 160
  • Journal:
    Journal of Molecular Biology
  • Volume:
    307
  • Issue:
    1
  • Print ISSN:
    0022-2836
  • Keywords:
    anti-DNA, anti-DNA antibodies, antibodies, Antibody, GENE, MB, Mutation, MUTATIONS, ABILITY, AFFINITIES, affinity, Amino Acid Sequence, anti-DNA, Antibodies, Antinuclear, Monoclonal, ANTIGEN, Antigens, ANTINUCLEAR, Arginine, BINDING, BINDING-SITE, CHAIN, chains, chemistry, Complementarity Determining Regions, Computer simulation, DNA, DNA binding, DNA-binding, enhanced, Enzyme-Linked Immunosorbent Assay, Form, Gene Expression, Genes, genetics, Germline, heavy chain, IgG, IM, IMMUNOGLOBULIN, Immunoglobulin Gene, IMMUNOGLOBULIN GENES, Immunoglobulin Variable Region, IMMUNOGLOBULINS, Immunoglobulins, Light-Chain, immunology, INCREASE, LA, LIGHT, LIGHT-CHAIN, metabolism, model, MODELS, Models, Molecular, Molecular Sequence Data, Molecule, MOLECULES, Mutagenesis, Site-Directed, Pattern, PATTERNS, Properties, Property, Protein Conformation, RANGE, REGION, regions, Rheumatology, SEQUENCE, Sequence Homology, Amino Acid, SEQUENCES, SITE, SITES, SPECIFICITIES, SPECIFICITY, Structure, Support, Non-U.S.Gov't, Three-dimensional, variable
  • Notes:
    UI - 21140168 LA - eng RN - 0 (Antibodies, Antinuclear) RN - 0 (Antibodies, Monoclonal) RN - 0 (Immunoglobulin Variable Region) RN - 0 (Immunoglobulins, Light-Chain) RN - 9007-49-2 (DNA) PT - Journal Article DA - 20010313 IS - 0022-2836 SB - IM CY - England
Abstract
2a2 is the most commonly rearranged gene in the human V(lambda )locus. It has been postulated that certain immunoglobulin genes (including 2a2) are rearranged preferentially because their germline sequences encode structures capable of binding to a range of antigens. Somatic mutation could then increase the specificity and affinity of binding to a particular antigen.We studied the properties of five IgG molecules in which the same heavy chain was paired with different light chains derived from 2a2. The pattern of somatic mutations in 2a2 was shown to be crucial in conferring the ability to bind DNA, but two different patterns of mutation each conferred this ability.Computer-generated models of the three-dimensional structures of these antibodies illustrate the ability of 2a2 to form a DNA binding site in different ways. Somatic mutations at the periphery of the DNA binding site were particularly important. In two different light chains, mutations to arginine at different sites in the complementarity determining regions (CDRs) enhanced binding to DNA. In a third light chain, however, mutation to arginine at a different site blocked binding to DNA
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