[HTML][HTML] Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of residues that determine agonist selectivity
RJ Prince, SM Sine - Journal of Biological Chemistry, 1996 - ASBMB
Agonists and antagonists select between the αγ and αδ binding sites of the fetal muscle
acetylcholine receptor owing to different contributions by the γ and δ subunits. To identify
determinants of selectivity for agonists, we constructed a panel of γ-δ subunit chimeras, co-
expressed them with the α subunit in 293 HEK cells, and measured carbamylcholine binding
affinity of intracellular complexes. Wild-type αδ complexes bind carbamylcholine about 30-
fold more tightly than αγ complexes. This degree of selectivity is similar to that of the resting …
acetylcholine receptor owing to different contributions by the γ and δ subunits. To identify
determinants of selectivity for agonists, we constructed a panel of γ-δ subunit chimeras, co-
expressed them with the α subunit in 293 HEK cells, and measured carbamylcholine binding
affinity of intracellular complexes. Wild-type αδ complexes bind carbamylcholine about 30-
fold more tightly than αγ complexes. This degree of selectivity is similar to that of the resting …