ArticleProceedings of the National Academy of Sciences of the United States of America1993
26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
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- Structural basis for DNA strand separation by a hexameric replicative helicase.Nucleic acids research · 2015Article
- Cell surface display yields evolvable, clickable antibody fragments.Chembiochem : a European journal of chemical biology · 2014Article
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- Steered molecular dynamics simulations of ligand-receptor interaction in lipocalins.European biophysics journal : EBJ · 2011Article
- Molecular similarity methods for predicting cross-reactivity with therapeutic drug monitoring immunoassays.Therapeutic drug monitoring · 2009Article
- Chemoinformatic methods for predicting interference in drug of abuse/toxicology immunoassays.Clinical chemistry · 2009Article
- Closely related antibody receptors exploit fundamentally different strategies for steroid recognition.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Synthetic antibody libraries focused towards peptide ligands.Journal of molecular biology · 2008Article
- Effects of mutation at the D-JH junction on affinity, specificity, and idiotypy of anti-progesterone antibody DB3.Protein science : a publication of the Protein Society · 2006Article
- Modifying specificity of antidigoxin antibodies using insertional mutagenesis.Protein science : a publication of the Protein Society · 2002Article
- On the calculation of absolute macromolecular binding free energies.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production.Applied and environmental microbiology · 2002Article
- Steroid binding by antibodies and artificial receptors: exploration of theoretical methods to determine the origins of binding affinities and specificities.Journal of computer-aided molecular design · 2000Article
- The structural basis of repertoire shift in an immune response to phosphocholine.The Journal of experimental medicine · 2000Article
- Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Antibody immunodiversity: a study on the marked specificity difference between two anti-yeast iso-1 cytochrome c monoclonal antibodies whose epitopes are closely related.Journal of protein chemistry · 1999Article
- In vitro scanning saturation mutagenesis of an antibody binding pocket.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
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9 authors.
Funding
Abstract
We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 A resolution and as a complex with digoxin at 2.5 A resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.
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