In the current chapter, we review approaches to the identification of the residues forming the
binding sites for agonists, antagonists, and allosteric modulators in the family of aminergic G …

During the past few years, crystallography of G protein–coupled receptors (GPCRs) has
experienced exponential growth, resulting in the determination of the structures of 16 distinct …

G protein-coupled receptors (GPCRs) comprise the most 'prolific'family of cell membrane
proteins, which share a general mechanism of signal transduction, but greatly vary in ligand …

Structural studies on G protein-coupled receptors (GPCRs) provide important insights into
the architecture and function of these important drug targets. However, the crystallization of …

Based on indications of direct physical interactions between neuropeptide and monoamine
receptors in the early 1980s, the term receptor–receptor interactions was introduced and …

The second extracellular (E2) loop of G protein-coupled receptors (GPCRs) plays an
essential but poorly understood role in the binding of non-peptidic small molecules. We …

G protein–coupled receptors (GPCRs) are integral membrane proteins that represent an
important class of drug targets. In particular, aminergic GPCRs interact with a significant …

The aminergic family of G protein-coupled receptors (GPCRs) plays an important role in
various diseases and represents a major drug discovery target class. Structure …

The superfamily of G protein‐coupled receptors (GPCRs) is the largest and most diverse
group of transmembrane proteins involved in signal transduction. Many of the over 1000 …

Crucial as molecular sensors for many vital physiological processes, seven-transmembrane
domain G protein-coupled receptors (GPCRs) comprise the largest family of proteins …