Abstract
Over the last two decades, an increasing number of studies have been devoted to the understanding of the molecular mechanism involved in the binding of different agonists and antagonists to β2-adrenergic receptor (β2AR) inactive and active conformations. The active-state 3.2 Å X-ray crystal structure of the human β2AR in complex with the endogenous low affinity agonist adrenaline represents an optimal starting structure for the analysis of the binding of different catecholamines to adrenergic receptors.
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