Abstract
A metalloantibody has been constructed with a coordination site for metals in the antigen binding pocket. The Zn(II) binding site from carbonic anhydrase B was used as a model. Three histidine residues have been placed in the light chain complementarity determining regions of a single chain antibody molecule. In contrast to the native protein, the mutant displayed metal-dependent fluorescence-quenching behavior. This response was interpreted as evidence for metal binding in the three-histidine site with relative affinities in the order Cu(II) > Zn(II) > Cd(II). The presence of metal cofactors in immunoglobulins should facilitate antibody catalysis of redox and hydrolytic reactions.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 5:24 a.m.) |
Indexed | 1 month, 3 weeks ago (July 8, 2025, 10:07 a.m.) |
Issued | 35 years ago (Aug. 10, 1990) |
Published | 35 years ago (Aug. 10, 1990) |
Published Print | 35 years ago (Aug. 10, 1990) |
@article{Iverson_1990, title={Metalloantibodies}, volume={249}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2116666}, DOI={10.1126/science.2116666}, number={4969}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Iverson, Brent L. and Iverson, Sheila A. and Roberts, Victoria A. and Getzoff, Elizabeth D. and Tainer, John A. and Benkovic, Stephen J. and Lerner, Richard A.}, year={1990}, month=aug, pages={659–662} }