Residues 1 to 80 of the N-terminal domain of the β 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 β subunit confer neuronal bungarotoxin sensitivity and agonist selectivity on neuronal nicotinic receptors. Federation of European Biochemical Societies (FEBS) Letters, 332, (1-2), 139-142. (doi:10.1016/0014-5793(93)80500-T).
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Description/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 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.
| Item Type: | Article |
|---|---|
| ISSNs: | 0014-5793 (print) |
| Related URLs: | |
| Keywords: | nicotinic receptor, chimeric subunit, xenopus oocyte, neuronal bungarotoxin |
| Subjects: | Q Science > Q Science (General) Q Science > QR Microbiology |
| Divisions: | University Structure - Pre August 2011 > School of Biological Sciences |
| Item ID: | 56763 |
| Date Deposited: | 22 Aug 2008 |
| Last Modified: | 02 Mar 2012 13:32 |
| Contributors: | Wheeler, Susan V. (Author) Chad, John E. (Author) Foreman, Richard (Author) |
| Date: | 11 October 1993 |
| Status: | Published |
| URI: | http://eprints.soton.ac.uk/id/eprint/56763 |
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