The mongoose acetylcholine receptor α-subunit: Analysis of glycosylation and α-bungarotoxin binding

Orna Asher, Bo S. Jensen, Monica Lupu-Meiri, Yoram Oron, Sara Fuchs

Research output: Contribution to journalArticlepeer-review

Abstract

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 a- 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.

Original languageEnglish
Pages (from-to)212-216
Number of pages5
JournalFEBS Letters
Volume426
Issue number2
DOIs
StatePublished - 17 Apr 1998

Keywords

  • Acetylcholine receptor
  • Glycosylation
  • Mongoose
  • α- Bungarotoxin
  • α-Subunit

Fingerprint

Dive into the research topics of 'The mongoose acetylcholine receptor α-subunit: Analysis of glycosylation and α-bungarotoxin binding'. Together they form a unique fingerprint.

Cite this