NDLI: The Functional Architecture of an Acetylcholine Receptor-mimicking Antibody

Content Provider	Journal of Biological Chemistry (JBC)
Author	Mérienne, Karine Germain, Nathalie Zinn-Justin, Sophie Boulain, Jean-Claude Ducancel, Frédéric Ménez, André
Abstract	Mα2-3 is a monoclonal antibody that partially mimics the nicotinic acetylcholine receptor (AChR). Its three-dimensional structure has been previously predicted by molecular modeling, suggesting that 29 complementarity determining region (CDR) residues and 2 framework residues are exposed to solvent. To identify the antibody residues that bind to the antigen, i.e. snake toxin that binds specifically to AChR, we (i) produced the scFv form of Mα2-3 fused to alkaline phosphatase, in the periplasmic space ofEscherichia coli; (ii) submitted approximately 75% of exposed residues of the fused scFv to individual or combined mutations, and (iii) identified the residues whose mutations affect scFv binding to the toxin, using a sensitive enzyme-linked immunosorbent assay. 11 critical residues were identified, including 8 heavy chain residues, 2 framework residues, and 1 light chain residue. They cover a surface of approximately 800 Å2, with a subset of most critical residues (VHD31, VHY32, and VHG101) and several aromatic residues. This functional architecture not only constitutes a plausible complementary binding surface for the snake toxin but also offers a structural basis to ultimately understand the capacity of the antibody to partially mimic AChR.
Related Links	http://www.jbc.org/content/272/38/23775.abstract
Ending Page	23783
Starting Page	23775
Page Count	9
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	38
Volume Number	272
DOI	10.1074/jbc.272.38.23775
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1997-09-19
Access Restriction	Open
Subject Keyword	PROTEIN CHEMISTRY AND STRUCTURE
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Mimicry between Receptors and Antibodies IDENTIFICATION OF SNAKE TOXIN DETERMINANTS RECOGNIZED BY THE ACETYLCHOLINE RECEPTOR AND AN ACETYLCHOLINE RECEPTOR-MIMICKING MONOCLONAL ANTIBODY

Molecular and Structural Basis of the Specificity of a Neutralizing Acetylcholine Receptor-mimicking Antibody, Using Combined Mutational and Molecular Modeling Analyses

The Drosophila Acetylcholine Receptor Subunit Dα5 Is Part of an α-Bungarotoxin Binding Acetylcholine Receptor

Creating an α7 Nicotinic Acetylcholine Recognition Domain from the Acetylcholine-binding Protein CRYSTALLOGRAPHIC AND LIGAND SELECTIVITY ANALYSES

Structural Effects of Neutral and Anionic Lipids on the Nicotinic Acetylcholine Receptor AN INFRARED DIFFERENCE SPECTROSCOPY STUDY

A New Family of Conus Peptides Targeted to the Nicotinic Acetylcholine Receptor

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Structural and Functional Characterization of a Novel Homodimeric Three-finger Neurotoxin from the Venom of Ophiophagus hannah (King Cobra)

Probing the Structure of the Nicotinic Acetylcholine Receptor Ion Channel with the Uncharged Photoactivable Compound [3H]Diazofluorene

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