Stabilization of bound polycyclic aromatic hydrocarbons by a pi-cation interaction

Autor: Bitao Zhao, Victoria A. Roberts, Hui-I. Kao, Jean-Luc Pellequer, Kai Li, Alexander E. Karu, Christopher W. Bell, Qing X. Li
Přispěvatelé: The Scripps Research Institute [La Jolla], University of California [San Diego] (UC San Diego), University of California-University of California, University of California [Berkeley], University of California, University of Hawaii
Rok vydání: 2000
Předmět:
Models
Molecular
Molecular model
Stereochemistry
protein mutagenesis
Static Electricity
Immunoglobulin Variable Region
Enzyme-Linked Immunosorbent Assay
Antigen-Antibody Complex
010402 general chemistry
Arginine
Ligands
01 natural sciences
03 medical and health sciences
chemistry.chemical_compound
Mice
Molecular recognition
Structural Biology
Cations
Static electricity
Benzo(a)pyrene
Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
Binding site
Molecular Biology
030304 developmental biology
0303 health sciences
cation-π interaction
antibody-antigen complex
Base Sequence
Chemistry
molecular modeling
Lysine
Mutagenesis
Cationic polymerization
Antibodies
Monoclonal
Ligand (biochemistry)
0104 chemical sciences
Amino Acid Substitution
Mutation
Mutagenesis
Site-Directed
Pyrene
Thermodynamics
molecular recognition
Binding Sites
Antibody
Haptens
Zdroj: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2000, 302 (3), pp.691-699. ⟨10.1006/jmbi.2000.4033⟩
ISSN: 0022-2836
1089-8638
Popis: International audience; Proteins can use aromatic side-chains to stabilize bound cationic ligands through cation-p interactions. Here, we report the ®rst example of the reciprocal process, termed p-cation, in which a cationic protein side-chain stabilizes a neutral aromatic ligand. Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene. This Arg was very likely selected for in the primary response, further underscoring the importance of the p-cation interaction for ligand binding, which should be considered in protein analysis and design when ligands include aromatic groups.
Databáze: OpenAIRE
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