Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870023 | FEBS Letters | 2014 | 7 Pages |
Abstract
Despite the physiological and pharmacological importance of the α1A-adrenoreceptor, the mode of interactions of classical agonists and radioactive ligands with this receptor is not yet clearly defined. Here, we used mutagenesis studies and binding experiments to evaluate the importance of 11 receptor sites for the binding of 125I-HEAT, 3H-prazosin and epinephrine. Only one residue (F312) commonly interacts with the three molecules, and, surprisingly, D106 interacts only with epinephrine in a moderate way. Our docking model shows that prazosin and HEAT are almost superimposed into the orthosteric pocket with their tetralone and quinazoline rings close to the phenyl ring of the agonist.
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Authors
Arhamatoulaye Maïga, Mélanie Dupont, Guillaume Blanchet, Elodie Marcon, Bernard Gilquin, Denis Servent, Nicolas Gilles,