 |
PDBsum entry 1kel
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Catalytic antibody
|
PDB id
|
|
|
|
1kel
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-Angstrom resolution.
|
|
|
Authors
|
|
L.C.Hsieh-Wilson,
P.G.Schultz,
R.C.Stevens.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 1996,
93,
5363-5367.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The x-ray crystal structures of the sulfide oxidase antibody 28B4 and of
antibody 28B4 complexed with hapten have been solved at 2.2-angstrom and
1.9-angstrom resolution, respectively. To our knowledge, these structures are
the highest resolution catalytic antibody structures to date and provide insight
into the molecular mechanism of this antibody-catalyzed monooxygenation
reaction. Specifically, the data suggest that entropic restriction plays a
fundamental role in catalysis through the precise alignment of the thioether
substrate and oxidant. The antibody active site also stabilizes developing
charge on both sulfur and periodate in the transition state via cation-pi and
electrostatic interactions, respectively. In addition to demonstrating that the
active site of antibody 28B4 does indeed reflect the mechanistic information
programmed in the aminophosphonic acid hapten, these high-resolution structures
provide a basis for enhancing turnover rates through mutagenesis and improved
hapten design.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
An efficient antibody-Catalyzed monooxygenation reaction
|
|
|
Authors
|
|
L.C.Hsieh,
J.C.Stephans,
P.G.Schultz.
|
|
|
Ref.
|
|
j am chem soc, 1994,
116,
2167.
|
|
|
|
|
|
|
|
