title: Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor.
abstract: 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.
authors.affiliation: Division of Physical Biochemistry, National Institute for Medical Research, London, UK.
authors.forename: E C
authors.initials: EC
authors.lastname: Hulme
authors.forename: Z L
authors.initials: ZL
authors.lastname: Lu
mesh_terms: D000818:Animals; D019556:COS Cells; D016296:Mutagenesis / Q000502:physiology*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011976:Receptors, Muscarinic / Q000737:chemistry* / Q000235:genetics
chemical_list: D011976:Receptors, Muscarinic