The mongoose acetylcholine receptor α‐subunit: analysis of glycosylation and α‐bungarotoxin binding

FEBS Letters

Jensen, Bo S¹  Lupu-Meiri, Monica²  Fuchs, Sara¹  Asher, Orna¹  Oron, Yoram² 

[1] Department of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel;Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel

关键词: Acetylcholine receptor;    α-Subunit;    Glycosylation;    α-Bungarotoxin;    Mongoose;   

DOI  :  10.1016/S0014-5793(98)00341-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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

【 授权许可】

Unknown