Agonist-driven conformational changes in the inner beta-sheet of alpha7 nicotinic receptors.

@article{McLaughlin2007AgonistdrivenCC,
  title={Agonist-driven conformational changes in the inner beta-sheet of alpha7 nicotinic receptors.},
  author={James T. McLaughlin and Jie Fu and Robert L. Rosenberg},
  journal={Molecular pharmacology},
  year={2007},
  volume={71 5},
  pages={1312-8}
}
Cys-loop ligand-gated ion channels assemble as pentameric proteins, and each monomer contributes two structural elements: an extracellular ligand-binding domain (LBD) and a transmembrane ion channel domain. Models of receptor activation include rotational movements of subunits leading to opening of the ion channel. We tested this idea using substituted cysteine accessibility to track conformational changes in the inner beta sheet of the LBD. Using a nondesensitizing chick alpha7 background (L… CONTINUE READING