Fundamental difference between the molecular interactions of agonists and antagonists with the beta-adrenergic receptor.
Antagonist binding to the beta-adrenergic receptor is largely entropy driven, with only a small enthalpy component. The binding of agonists, on the other hand, is associated with a large decrease in enthalpy which permits a highly unfavourable decrease in entropy. The thermodynamic differences between the binding of agonists and antagonists may provide new insights into the molecular basis for hormone stimulation of adenylate cyclase activity.
D000262:Adenylyl Cyclases / Q000097:blood; D000318:Adrenergic beta-Agonists / Q000378:metabolism*; D000319:Adrenergic beta-Antagonists / Q000378:metabolism*; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000378:metabolism; D008024:Ligands; D011941:Receptors, Adrenergic / Q000378:metabolism*; D011943:Receptors, Adrenergic, beta / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics; D014422:Turkeys
D000318:Adrenergic beta-Agonists; D000319:Adrenergic beta-Antagonists; D008024:Ligands; D011941:Receptors, Adrenergic; D011943:Receptors, Adrenergic, beta; D000262:Adenylyl Cyclases