Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor.
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.
Hulme
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Division of Physical Biochemistry, National Institute for Medical Research, London, UK.
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D000818:Animals; D019556:COS Cells; D016296:Mutagenesis / Q000502:physiology*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011976:Receptors, Muscarinic / Q000737:chemistry* / Q000235:genetics
D011976:Receptors, Muscarinic