The acetylcholine receptor (AChR) from vertebrate skeletal muscle is a pentamer composed of two ligand-binding α-subunits and one β-, γ-, and δ-subunit. To examine the functional roles of the non-α-subunits, we have expressed, in stable cell lines, AChRs lacking either a γ- or a δ-subunit. Most previous work has examined how these changes in subunit composition affect single channel properties. Here, we take advantage of the stable expression system to produce large amounts of AChR and, for the first time, examine ligand binding to altered AChRs on intact cells. The changes in subunit composition affect both ligand affinity and cooperativity of the receptor, suggesting important roles for the γ- and δ-subunits, both in shaping the ligand binding site and maintaining cooperative interactions between α-subunits.
|Original language||English (US)|
|Number of pages||9|
|Journal||Journal of Biological Chemistry|
|State||Published - Jan 1 1991|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology