Final answer:
G-protein-coupled receptors (GPCRs) have seven transmembrane domains and three tethered subunits. The α subunit is bound to GDP, which is exchanged for GTP upon stimulation. GTPase inhibits the intrinsic GTPase activity of the α subunit.
Step-by-step explanation:
G-protein-coupled receptors (GPCRs) all have a similar structure with seven transmembrane domains. When a GPCR binds an extracellular signal, an intracellular G protein, composed of three subunits, becomes activated.
Three of the G-protein subunits are tethered to the plasma membrane by short lipid tails. When unstimulated, the α subunit is bound to GDP, which is exchanged for GTP on stimulation.
The intrinsic GTPase activity of the α subunit is important for inactivating the G protein. GTPase inhibits this activity of the α subunit, thereby keeping the subunit in an active state.