Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors

@inproceedings{daCosta2015StoichiometryF,
  title={Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors},
  author={Corrie J. B. daCosta and Chris R. Free and Steven M. Sine},
  booktitle={Nature communications},
  year={2015}
}
α-Bungarotoxin (α-Btx) binds to the five agonist binding sites on the homopentameric α7-acetylcholine receptor, yet the number of bound α-Btx molecules required to prevent agonist-induced channel opening remains unknown. To determine the stoichiometry for α-Btx blockade, we generate receptors comprised of wild-type and α-Btx-resistant subunits, tag one of the subunit types with conductance mutations to report subunit stoichiometry, and following incubation with α-Btx, monitor opening of… CONTINUE READING
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