5NBW

Crystal structure of the Fab fragment 22F12 in complex with 3-hydroxybenzo[a]pyrene

5NBW の概要

• エントリーDOI: 10.2210/pdb5nbw/pdb
• 分子名称: Fab 22F12 (L,H), Fab 22F12 (A,B), benzo[a]pyren-3-ol, ... (4 entities in total)
• 機能のキーワード: antibody, benzo[a]pyrene, fab fragment, hapten, immune system
• 由来する生物種: Mus musculus (House Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96609.25

構造登録者

Skerra, A.,Eichinger, A. (登録日: 2017-03-02, 公開日: 2017-06-28, 最終更新日: 2024-10-23)

主引用文献

Eichinger, A.,Neumaier, I.,Pschenitza, M.,Niessner, R.,Knopp, D.,Skerra, A.
Tight Molecular Recognition of Benzo[a]pyrene by a High-Affinity Antibody.
Angew. Chem. Int. Ed. Engl., 56:10592-10597, 2017

PubMed Abstract: Benzo[a]pyrene, which is produced during the incomplete combustion of organic material, is an abundant noxious pollutant because of its carcinogenic metabolic degradation products. The high-affinity (K ≈3 nm) monoclonal antibody 22F12 allows facile bioanalytical quantification of benzo[a]pyrene even in complex matrices. We report the functional and X-ray crystallographic analysis of 22F12 in complex with 3-hydroxybenzo[a]pyrene after cloning of the V-genes and production as a recombinant Fab fragment. The polycyclic aromatic hydrocarbon is bound in a deep pocket between the light and heavy chains, surrounded mainly by aromatic and aliphatic amino acid side chains. Interestingly, the hapten-antibody interface is less densely packed than expected and reveals polar, H-bond-like interactions with the polycyclic aromatic π-electron system, which may allow the antibody to maintain a large, predominantly hydrophobic binding site in an aqueous environment while providing sufficient complementarity to its ligand.

PubMed: 28603847
DOI: 10.1002/anie.201703893

実験手法

X-RAY DIFFRACTION (2.4 Å)