26-10 Fab-digoxin complex: Affinity and specificity due to surface complementarity
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 Å resolution and as a complex with digoxin at 2.5 Å 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.
Additional Information
© 1993 National Academy of Sciences. Communicated by David R. Davies, June 24, 1993. We thank Drs. Joel Schildbach, Robert Bruccoleri, and Jiri Novotny for helpful discussions and Dr. Martha Ludwig for the use of her data collection facility. This work was supported in part by National Institutes of Health Grants PO1-HL19259 and RO1-HL47415.Attached Files
Published - PNAS-1993-Jeffrey-10310-4.pdf
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Additional details
- PMCID
- PMC47764
- Eprint ID
- 52869
- Resolver ID
- CaltechAUTHORS:20141216-113004558
- PO1-HL19259
- NIH
- RO1-HL47415
- NIH
- Created
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2014-12-16Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field