ArticleProceedings of the National Academy of Sciences of the United States of America1989
Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: proposal of a structural mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 58 citations in OpenAlex.
- A Sitewise Model of Natural Selection on Individual Antibodies via a Transformer-Encoder.Molecular biology and evolution · 2025Article
- A novel computer algorithm improves antibody epitope prediction using affinity-selected mimotopes: a case study using monoclonal antibodies against the West Nile virus E protein.Molecular immunology · 2008Article
- The structural basis of repertoire shift in an immune response to phosphocholine.The Journal of experimental medicine · 2000Article
- Mass spectrometric measurement of changes in protein hydrogen exchange rates that result from point mutations.Journal of the American Society for Mass Spectrometry · 1996Article
- Enhancement and destruction of antibody function by somatic mutation: unequal occurrence is controlled by V gene combinatorial associations.The EMBO journal · 1995Article
- Mutational analysis of an autoantibody: differential binding and pathogenicity.The Journal of experimental medicine · 1994Article
- Structural properties of a subset of nephritogenic anti-DNA antibodies.Immunologic research · 1994Article
- Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region.Journal of protein chemistry · 1993Article
- Modulation of antibody affinity by a non-contact residue.Protein science : a publication of the Protein Society · 1993Article
- Generation and analysis of random point mutations in an antibody CDR2 sequence: many mutated antibodies lose their ability to bind antigen.The Journal of experimental medicine · 1992Article
- Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Altered reactivity of immunoglobulin produced by human-human hybridoma cells transfected by pSV2-neo gene.Cytotechnology · 1991Article
- Characterization of somatically mutated S107 VH11-encoded anti-DNA autoantibodies derived from autoimmune (NZB x NZW)F1 mice.The Journal of experimental medicine · 1991Article
- Antibody remodeling: a general solution to the design of a metal-coordination site in an antibody binding pocket.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
- New nucleotide sequence data on the EMBL File Server.Nucleic acids research · 1989Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To study the molecular basis for antibody diversity and the structural basis for antigen binding, we have characterized the loss of phosphocholine (P-Cho) binding both experimentally and computationally in U10, a somatic mutant of the antibody S107. Nucleotide sequencing of U10 shows a single base change in JH1, substituting Asp-101 with Ala, over 9 A distant from the P-Cho-binding pocket. Probing with antiidiotypic antibodies suggests local, not global, conformational changes. Computational results support a specific structural mechanism for the loss of P-Cho binding. The U10 mutation eliminates the charged interaction between Asp-101 and Arg-94, which allows the Arg-94 side chain to disrupt P-Cho binding sterically and electrostatically by folding into the P-Cho-binding site. These results specifically show the importance of the Arg-94 to Asp-101 side chain salt bridge in the heavy-chain CDR3 conformation and suggest that residues distant from the binding site play an important role in antibody diversity and inducible complementarity.
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