Page_1995_Eur.J.Pharmacol_289_429

Reference

Title : The functional role of the binding site aspartate in muscarinic acetylcholine receptors, probed by site-directed mutagenesis - Page_1995_Eur.J.Pharmacol_289_429
Author(s) : Page KM , Curtis CA , Jones PG , Hulme EC
Ref : European Journal of Pharmacology , 289 :429 , 1995
Abstract :

Mutation of the Asp in transmembrane domain three of the muscarinic receptors to Asn (M1) or Glu (M1 and M2) strongly reduced the high-affinity component of agonist binding, and the M1 phosphoinositide response. Formation of the acetylcholine-receptor binary complex was also strongly inhibited. In contrast, binary complex formation by other agonists, as well as the antagonist (-)-N-methylscopolamine, was less affected. Ionic bonding between the carboxylate oxyanion and the positively-charged headgroup probably anchors acetylcholine when it is bound in its active conformation, but alternative, non-productive, binding modes, promoted by non-polar forces, may contribute to binary complex formation by other ligands.

PubMedSearch : Page_1995_Eur.J.Pharmacol_289_429
PubMedID: 7556411

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Citations formats

Page KM, Curtis CA, Jones PG, Hulme EC (1995)
The functional role of the binding site aspartate in muscarinic acetylcholine receptors, probed by site-directed mutagenesis
European Journal of Pharmacology 289 :429

Page KM, Curtis CA, Jones PG, Hulme EC (1995)
European Journal of Pharmacology 289 :429