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• W2078905154 abstract "Three-dimensional structural models of six murine anti-(H2A-H2B) monoclonal autoantibody variable fragments were built by comparative molecular modeling using the COMPOSER software. Analysis of the antibody combining sites is based on the hypothesis that ionic and/or electrostatic interactions predominate in antigen-antibody binding, as suggested by the cationic nature of histones and the amino acid sequences of the antibody hypervariable regions. The study of the electrostatic potentials of their combining site surfaces, computed with the MOLCAD software, and the comparison with the electrostatic potentials of 13 selected control mAbs show the lack of a unique electrostatic pattern. One group of three mAbs expresses a strong and large electronegative area, supporting the hypothesis that ionic interactions predominate in antigen recognition. The second group, containing the other three mAbs, exhibits an alternation of electropositive and electronegative areas. All, however, present a localized electronegative area in the vicinity of H-CDR1 and H-CDR2 loops that is generated by the presence of at least one acidic residue. The model suggesting that the binding activity may depend on charged residues at the same site is reminiscent of what was previously reported in anti-DNA mAbs. In addition, the alternation of electropositive areas and electronegative areas in second group mAbs is also frequently observed in certain anti-DNA mAbs. These data argue for the existence of relationships between these two autoantibody populations and suggest that they share a common immunogenic particle formed by anionic and cationic components, such as a nucleosome." @default.
• W2078905154 created "2016-06-24" @default.
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• W2078905154 date "1997-08-01" @default.
• W2078905154 modified "2023-10-18" @default.
• W2078905154 title "Modeling of anti-nucleosome immunoglobulin Fv domains: Analysis of electrostatic interactions" @default.
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• W2078905154 doi "https://doi.org/10.1016/s0161-5890(97)00059-x" @default.
• W2078905154 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9444978" @default.
• W2078905154 hasPublicationYear "1997" @default.
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