5NBW

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

Summary for 5NBW

• Entry DOI: 10.2210/pdb5nbw/pdb
• Descriptor: Fab 22F12 (L,H), Fab 22F12 (A,B), benzo[a]pyren-3-ol, ... (4 entities in total)
• Functional Keywords: antibody, benzo[a]pyrene, fab fragment, hapten, immune system
• Biological source: Mus musculus (House Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 96609.25

Authors

Skerra, A.,Eichinger, A. (deposition date: 2017-03-02, release date: 2017-06-28, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)