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Updated: Apr 11, 2026

Extracellular Multi-Unit Recording from the Olfactory Nerve of Teleosts

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Published on: October 6, 2020

From shellfish poisoning to neuroscience.

Azadeh Shahsavar¹, Thomas Balle²

¹Danish Research Institute of Translational Neuroscience - DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.

Structure (London, England : 1993)

|June 4, 2015

Summary

This summary is machine-generated.

Researchers determined X-ray structures of acetylcholine binding protein (AChBP) complexed with pinnatoxins. This structural insight may aid in developing novel central nervous system (CNS)-penetrant nicotinic acetylcholine receptor (nAChR) antagonists.

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Area of Science:

Structural Biology
Neuroscience
Pharmacology

Background:

Acetylcholine binding protein (AChBP) serves as a model for nicotinic acetylcholine receptors (nAChRs).
Phycotoxins, such as pinnatoxins, are potent neurotoxins that interact with nAChRs.
Understanding toxin-receptor interactions is crucial for developing targeted therapeutics.

Purpose of the Study:

To elucidate the structural basis of pinnatoxin binding to AChBP.
To provide insights into the molecular mechanisms of phycotoxin action.
To inform the design of novel nAChR modulators.

Main Methods:

X-ray crystallography was employed to determine the structures of AChBP-pinnatoxin complexes.
Detailed structural analysis was performed to characterize the binding interfaces.

Main Results:

The study reports high-resolution X-ray structures of AChBP in complex with two distinct pinnatoxins.
Structural data reveals specific interactions between the phycotoxins and the ligand-binding domain of AChBP.
The binding modes provide a molecular understanding of pinnatoxin's potent activity.

Conclusions:

The determined structures offer a foundation for understanding pinnatoxin-AChBP interactions.
These findings may guide the development of new CNS-penetrant and subtype-selective nAChR antagonists.
This research contributes to the broader field of neuropharmacology and toxin research.