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. 1998 Apr 17;426(2):212-6.
doi: 10.1016/s0014-5793(98)00341-x.

The Mongoose Acetylcholine Receptor Alpha-Subunit: Analysis of Glycosylation and Alpha-Bungarotoxin Binding

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The Mongoose Acetylcholine Receptor Alpha-Subunit: Analysis of Glycosylation and Alpha-Bungarotoxin Binding

O Asher et al. FEBS Lett. .
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Abstract

The mongoose AChR alpha-subunit has been cloned and shown to be highly homologous to other AChR alpha-subunits, with only six differences in amino acid residues at positions that are conserved in animal species that bind alpha-bungarotoxin (alpha-BTX). Four of these six substitutions cluster in the ligand binding site, and one of them, Asn-187, forms a consensus N-glycosylation site. The mongoose glycosylated alpha-subunit has a higher apparent molecular mass than that of the rat glycosylated alpha-subunit, probably resulting from the additional glycosylation at Asn-187 of the mongoose subunit. The in vitro translated mongoose alpha-subunit, in a glycosylated or non-glycosylated form, does not bind alpha-BTX, indicating that lack of alpha-BTX binding can be achieved also in the absence of glycosylation.

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