Three-dimensional structure of an idiotope–anti-idiotope complex
| Autor: | M.-M. Riottot, Graham A. Bentley, Roberto J. Poljak, G. Boulot |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Idiotype
Genetics Multidisciplinary Molecular Structure biology Protein Conformation Spatial structure Stereochemistry Chemistry Antibodies Monoclonal Hydrogen Bonding Idiotopes Antigen-Antibody Complex Epitope Antibodies Anti-Idiotypic Epitopes Molecular level Immunoglobulin Idiotypes Antigen Monoclonal biology.protein Muramidase Binding Sites Antibody Antibody Crystallization |
| Zdroj: | Nature. 348:254-257 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/348254a0 |
| Popis: | SEROLOGICALLY detected antigenic determinants unique to an antibody or group of antibodies1–3 are called idiotopes. The sum of idiotopes of an antibody constitute its idiotype3. Idiotypes have been intensively studied following a hypothesis for the self-regulation of the immune system through a network of idiotype–anti-idiotype interactions4. Furthermore, as antigen and anti-idiotypes can competitively bind to idiotype-positive, antigen-specific antibodies, anti-idiotypes may carry an 'internal image' of the external antigen (see refs 5–10 for reviews). Here we describe the structure of the complex between the monoclonal anti-lysozyme FabD1.3 and the anti-idiotopic FabE225 at 2.5 A resolution. This complex defines a private idiotope consisting of 13 amino-acid residues, mainly from the complementarity-determining regions of D1.3. Seven of these residues make contacts with the antigen, indicating a significant overlap between idiotope and antigen-combining site. Idiotopic mimicry of the external antigen is not achieved at the molecular level in this example. |
| Databáze: | OpenAIRE |
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