Metalloantibodies

Brent L. Iverson; Sheila A. Iverson; Victoria A. Roberts; Elizabeth D. Getzoff; John A. Tainer; Stephen J. Benkovic; Richard A. Lerner

Metalloantibodies

Brent L. Iverson, Sheila A. Iverson, Victoria A. Roberts, Elizabeth D. Getzoff, John A. Tainer, Stephen J. Benkovic, Richard A. Lerner

Chemistry

Research output: Contribution to journal › Article › peer-review

111 Scopus citations

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 hydfolytic reactions.

Original language	English (US)
Pages (from-to)	659-666
Number of pages	8
Journal	Science
Volume	249
Issue number	4969
State	Published - Aug 10 1990

All Science Journal Classification (ASJC) codes

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title = "Metalloantibodies",

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 hydfolytic reactions.",

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,

day = "10",

language = "English (US)",

volume = "249",

pages = "659--666",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "4969",

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TY - JOUR

T1 - Metalloantibodies

AU - Iverson, Brent L.

AU - Iverson, Sheila A.

AU - Roberts, Victoria A.

AU - Getzoff, Elizabeth D.

AU - Tainer, John A.

AU - Benkovic, Stephen J.

AU - Lerner, Richard A.

PY - 1990/8/10

Y1 - 1990/8/10

N2 - 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 hydfolytic reactions.

AB - 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 hydfolytic reactions.

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M3 - Article

C2 - 2116666

AN - SCOPUS:0025071847

SN - 0036-8075

VL - 249

SP - 659

EP - 666

JO - Science

JF - Science

IS - 4969

ER -

Metalloantibodies

Abstract

All Science Journal Classification (ASJC) codes

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