1KEL

CATALYTIC ANTIBODY 28B4 FAB FRAGMENT COMPLEXED WITH HAPTEN (1-[N-4'-NITROBENZYL-N-4'-CARBOXYBUTYLAMINO] METHYLPHOSPHONIC ACID)

1KEL の概要

• エントリーDOI: 10.2210/pdb1kel/pdb
• 分子名称: 28B4 FAB, 1-[N-4'-NITROBENZYL-N-4'-CARBOXYBUTYLAMINO]METHYLPHOSPHONIC ACID (3 entities in total)
• 機能のキーワード: sulfide oxidation, monooxygenase, oxygenation, fab, immunoglobulin, catalytic antibody
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Isoform Secreted: Secreted: P01868
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47732.10

構造登録者

Hsieh-Wilson, L.C.,Schultz, P.G.,Stevens, R.C. (登録日: 1996-04-16, 公開日: 1996-12-07, 最終更新日: 2024-11-20)

主引用文献

Hsieh-Wilson, L.C.,Schultz, P.G.,Stevens, R.C.
Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-angstrom resolution.
Proc.Natl.Acad.Sci.USA, 93:5363-5367, 1996

PubMed 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.

PubMed: 8643580
DOI: 10.1073/pnas.93.11.5363

実験手法

X-RAY DIFFRACTION (1.9 Å)