Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Metalloantibodies

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

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

publication date

  • August 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
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2116666

PubMed ID

  • 2116666
scroll to property group menus

Additional Document Info

start page

  • 659

end page

  • 662

volume

  • 249

issue

  • 4969

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support