| Title : The role of charge interactions in muscarinic agonist binding, and receptor-response coupling - Hulme_1995_Life.Sci_56(11-12)_891 |
| Author(s) : Hulme EC , Curtis CA , Page KM , Jones PG |
| Ref : Life Sciences , 56(11-12) :891 , 1995 |
| Abstract : Site-directed mutagenesis has been used to evaluate the roles of the key aspartate and arginine residues in transmembrane domain three of the muscarinic receptors. The results suggest that the formation of an ionic bond between the Asp carboxylate group and the onium headgroup is essential to anchor acetylcholine in its active, bound conformation in both binary agonist-receptor and ternary agonist-receptor-G-protein complexes, but that secondary, non-productive binding modes, promoted by non-polar forces, may contribute to binary complex formation by other ligands. The positive charge of the arginyl side-chain is central to the recognition, and subsequent activation of G-proteins by the agonist-M1 mAChR complex. |
| ESTHER : Hulme_1995_Life.Sci_56(11-12)_891 |
| PubMedSearch : Hulme_1995_Life.Sci_56(11-12)_891 |
| PubMedID: 10188790 |
Hulme EC, Curtis CA, Page KM, Jones PG (1995)
The role of charge interactions in muscarinic agonist binding, and receptor-response coupling
Life Sciences
56(11-12) :891
Hulme EC, Curtis CA, Page KM, Jones PG (1995)
Life Sciences
56(11-12) :891