The University of Southampton
University of Southampton Institutional Repository

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

Wheeler, Susan V., Chad, John E. and Foreman, Richard (1993) Residues 1 to 80 of the N-terminal domain of the ? subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors Febs Letters, 332, (1-2), pp. 139-142.

Record type: Article

Abstract

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 ? subunit is an important determinant of the receptor's pharmacological profile. Co-expression of ?4 and ?2 subunits produced a receptor that was relatively insensitive to cytisine and nicotine and inhibited by NBT, whilst the ?4?4 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 ? subunit are implicated in these characteristics, since the combination of ?4 with a hybrid ? subunit comprising amino acids 1 ? 80 of ?2 and 81 ? 416 of ?4 became relatively insensitive to nicotine and cytisine and resistant to inhibition by neuronal bungarotoxin.

Full text not available from this repository.

More information

Published date: 11 October 1993
Keywords: nicotinic receptor, chimeric subunit, xenopus oocyte, neuronal bungarotoxin

Identifiers

Local EPrints ID: 56763
URI: http://eprints.soton.ac.uk/id/eprint/56763
ISSN: 0014-5793
PURE UUID: 2ce6f15d-15c6-4852-9d66-d8822ef034c1
ORCID for John E. Chad: ORCID iD orcid.org/0000-0001-6442-4281

Catalogue record

Date deposited: 22 Aug 2008
Last modified: 16 Oct 2017 09:30

Export record

Contributors

Author: Susan V. Wheeler
Author: John E. Chad ORCID iD
Author: Richard Foreman

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×