Residues 1 to 80 of the N‐terminal domain of the β subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors

FEBS Letters

Wheeler, Susan V.¹  Foreman, Richard¹  Chad, John E.¹ 

[1] Department of Physiology and Pharmacology, University of Southampton, Bassett Crescent East, Southampton, SO9 3TU, UK

关键词: Nicotinic receptor;    Chimeric subunit;    Xenopus oocyte;    Neuronal bungarotoxin;   

DOI  :  10.1016/0014-5793(93)80500-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Standard two electrode voltage clamp techniques were used to investigate the response of neuronal nicotinic acetylcholine receptors, expressed in Xenopus oocytes, to various agonists and neuronal bungarotoxin (NBT). The β subunit is an important determinant of the receptor's pharmacological profile. Co-expression of α4 and β2 subunits produced a receptor that was relatively insensitive to cytisine and nicotine and inhibited by NBT, whilst the α4β4 combination produced a receptor that was highly sensitive to cytisine and nicotine but resistant to toxin. The first 80 amino acids of the N-terminal domain of the β subunit are implicated in these characteristics, since the combination of α4 with a hybrid β subunit comprising amino acids 1 → 80 of β2 and 81 → 416 of β4 became relatively insensitive to nicotine and cytisine and resistant to inhibition by neuronal bungarotoxin.

【 授权许可】

Unknown