Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor.

@article{Hulme1998ScanningMO,
  title={Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor.},
  author={Edward C. Hulme and Zhengrong Lu},
  journal={Journal of physiology, Paris},
  year={1998},
  volume={92 3-4},
  pages={269-74}
}
Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor has revealed a highly-differentiated alpha-helical structure. Lipid-facing residues are distinguished from a patch of residues which selectively stabilise the ground state of the receptor, and from a band of amino acids extending the full length of the helix, which contribute to the active agonist-receptor-G protein complex. The most important residues are strongly conserved in the GPCR superfamily.