Alpha-bungarotoxin Binding to Acetylcholine Receptor Membranes Studied by Low Angle X-ray Diffraction

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2003 Jul 30

PMID 12885641

Citations 16

Authors

Howard S Young

Leo G Herbette

Victor Skita

Affiliations

Soon will be listed here.

Abstract

The nicotinic acetylcholine receptor (nAChR) carries two binding sites for snake venom neurotoxins. alpha-Bungarotoxin from the Southeast Asian banded krait, Bungarus multicinctus, is a long neurotoxin which competitively blocks the nAChR at the acetylcholine binding sites in a relatively irreversible manner. Low angle x-ray diffraction was used to generate electron density profile structures at 14-A resolution for Torpedo californica nAChR membranes in the absence and presence of alpha-bungarotoxin. Analysis of the lamellar diffraction data indicated a 452-A lattice spacing between stacked nAChR membrane pairs. In the presence of alpha-bungarotoxin, the quality of the diffraction data and the lamellar lattice spacing were unchanged. In the plane of the membrane, the nAChRs packed together with a nearest neighbor distance of 80 A, and this distance increased to 85 A in the presence of toxin. Electron density profile structures were calculated in the absence and presence of alpha-bungarotoxin, revealing a location for the toxin binding sites. In native, fully-hydrated nAChR membranes, alpha-bungarotoxin binds to the nAChR outer vestibule and contacts the surface of the membrane bilayer.

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