A conserved disulfide loop facilitates conformational maturation in the subunits of the acetylcholine receptor
EC Walcott, K Sumikawa - Molecular brain research, 1996 - Elsevier
To examine the structural determinants for the assembly of ligand-gated receptors, we
constructed mutant α, β, γ and δ subunits of the Torpedo acetylcholine receptor (AChR),
lacking one of the conserved cysteine residues which forms a 13-amino acid disulfide loop
in the amino terminal domain of each subunit. Mutant subunits were co-expressed with
complementary wild-type subunits in Xenopus oocytes. Using subunit-specific antisera and
monoclonal antibodies that recognize the two distinct α-bungarotoxin (α-BuTX) sites on the …
constructed mutant α, β, γ and δ subunits of the Torpedo acetylcholine receptor (AChR),
lacking one of the conserved cysteine residues which forms a 13-amino acid disulfide loop
in the amino terminal domain of each subunit. Mutant subunits were co-expressed with
complementary wild-type subunits in Xenopus oocytes. Using subunit-specific antisera and
monoclonal antibodies that recognize the two distinct α-bungarotoxin (α-BuTX) sites on the …