TY - JOUR
T1 - γ- and δ-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor
AU - Sine, Steven M.
AU - Claudio, Toni
PY - 1991/10/15
Y1 - 1991/10/15
N2 - 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.
AB - 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.
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M3 - Article
C2 - 1680865
AN - SCOPUS:0026045588
SN - 0021-9258
VL - 266
SP - 19369
EP - 19377
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 29
ER -