Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias.

@article{Gregory2010IdentificationOO,
  title={Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias.},
  author={Karen J. Gregory and Nathan E. Hall and Andrew B. Tobin and Patrick M. Sexton and Arthur Christopoulos},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 10},
  pages={7459-74}
}
Muscarinic acetylcholine receptors contain at least one allosteric site that is topographically distinct from the acetylcholine, orthosteric binding site. Although studies have investigated the basis of allosteric modulation at these receptors, less is known about putative allosteric ligands that activate the receptor in their own right. We generated M(2) muscarinic acetylcholine receptor mutations in either the orthosteric site in transmembrane helices 3 and 6 (TM3 and -6) or part of an… CONTINUE READING

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