Abstract:
:The combination of complementary DNA expression and single-channel current analysis provides a powerful tool for studying the structure-function relationship of the nicotinic acetylcholine receptor (AChR) (refs 1-5). We have previously shown that AChR channels consisting of subunits from different species, expressed in the surface membrane of Xenopus oocytes, can be used to relate functional properties to individual subunits. Here we report that, in extracellular solution of low divalent cation concentration, the bovine AChR channel has a smaller conductance than the Torpedo AChR channel. Replacement of the delta-subunit of the Torpedo AChR by the bovine delta-subunit makes the channel conductance similar to that of the bovine AChR channel. To locate the region in the delta-subunit responsible for this difference, we have constructed chimaeric delta-subunit cDNAs with different combinations of the Torpedo and bovine counterparts. The conductances of AChR channels containing chimaeric delta-subunits suggest that a region comprising the putative transmembrane segment M2 and the adjacent bend portion between segments M2 and M3 is involved in determining the rate of ion transport through the open channel.
journal_name
Naturejournal_title
Natureauthors
Imoto K,Methfessel C,Sakmann B,Mishina M,Mori Y,Konno T,Fukuda K,Kurasaki M,Bujo H,Fujita Ydoi
10.1038/324670a0subject
Has Abstract,Author List Incompletepub_date
1986-12-18 00:00:00pages
670-4issue
6098eissn
0028-0836issn
1476-4687journal_volume
324pub_type
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