Profile of the α-bungarotoxin-binding regions on the extracellular part of the α-chain of Torpedo californica acetylcholine receptor

Author:

MULAC-JERIČEVIČ B1,Atassi M Z1

Affiliation:

1. Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030, U.S.A.

Abstract

The continuous alpha-neurotoxin-binding regions on the extracellular part (residues 1-210) of the alpha-chain of Torpedo californica acetylcholine receptor were localized by reaction of 125I-labelled alpha-bungarotoxin with synthetic overlapping peptides spanning this entire part of the chain. The specificity of the binding was confirmed by inhibition with unlabelled toxin and, for appropriate peptides, with unlabelled anti-(acetylcholine receptor) antibodies. Five toxin-binding regions were localized within residues 1-10, 32-41, 100-115, 122-150 and 182-198. The third, fourth and fifth (and to a lesser extent the first and second) toxin-binding regions overlapped with regions recognized by anti-(acetylcholine receptor) antibodies. The five toxin-binding regions may be distinct sites or, alternatively, different ‘faces’ in one (or more) sites.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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