Answer:
they bind to protein-coupled transmembrane receptors with higher complexity than those found in prokaryotes
Explanation:
G-proteins are proteins found inside the cells that function as molecular switches which are activated by binding to guanosine triphosphate (GTP), while they are inactive by binding to guanosine diphosphate (GDP). The G-proteins bind to G-protein-coupled transmembrane receptors (GPCRs) in the cytoplasmic region. The GPCRs are a very diverse group of proteins that are activated by extracellular molecules ranging from small peptides to large proteins, including pheromones, neurotransmitters, light-sensitive compounds, etc, thereby allowing them to respond to diverse stimuli from the extracellular environment. In consequence, it is reasonable to suppose that the signaling pathways in which G proteins are involved have a higher complexity level than those observed in primitive prokaryotic organisms.
Where’s the graph? You need to have the picture uploaded unless I’m just missing it.
The same ligand can bind to different receptors causing different responses (e.g.. acetylcholine). On the other hand, different ligands binding to different receptors can produce the same cellular response (e.g. glucagon, epinephrine).
