A conserved aspartic acid residue in transmembrane helix 3 of the muscarinic acetylcholine receptors is important in binding the headgroup of muscarinic ligands. This acidic amino acid probably points into a relatively hydrophilic cavity whose walls are formed by the amphipathic transmembrane helices of the receptor. Amino acid side chains within this cavity contribute to ligand binding.
|Number of pages||4|
|Journal||Trends in Pharmacological Sciences|
|Publication status||Published - 1 Dec 1989|
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