Metalloantibodies

Academic Article

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Overview

authors

• Iverson, B. L.
• Iverson, S. A.
• Roberts, V. A.
• Getzoff, Elizabeth
• Tainer, John
• Benkovic, S. J.
• Lerner, Richard

publication date

• 1990

journal

• Science  Journal

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) greater than Zn(II) greater than Cd(II). The presence of metal cofactors in immunoglobulins should facilitate antibody catalysis of redox and hydrolytic reactions.

subject areas

• Amino Acid Sequence
• Binding Sites, Antibody
• Cadmium
• Carbonic Anhydrases
• Copper
• Fluoresceins
• Immunoglobulin Heavy Chains
• Immunoglobulin Light Chains
• Ligands
• Metals
• Models, Molecular
• Molecular Sequence Data
• Protein Conformation
• Spectrometry, Fluorescence
• Zinc

Identity

International Standard Serial Number (ISSN)

• 0036-8075

Digital Object Identifier (DOI)

• 10.1126/science.2116666

PubMed ID

• 2116666

Additional Document Info

start page

• 659

end page

• 662

volume

• 249

issue

• 4969