Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand.

@article{Galzi1991AllostericTO,
  title={Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand.},
  author={J. L. Galzi and Fr{\'e}d{\'e}ric Revah and Françoise Bouet and Andr{\'e} M{\'e}nez and Maurice Goeldner and Christine Hirth and Jean Pierre Changeux},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1991},
  volume={88 11},
  pages={5051-5}
}
Structural changes occurring upon desensitization of the Torpedo marmorata acetylcholine receptor were monitored with tritiated p-(N,N-dimethyl)aminobenzenediazonium fluoroborate, a reversible competitive antagonist in the dark, which may serve as a photoaffinity probe of the area of the receptor molecule with which cholinergic ligands interact. Addition of meproadifen, an allosteric effector that stabilizes the high-affinity desensitized state of the receptor upon binding to a site… CONTINUE READING
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