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The seven-transmembrane α-helix structure of bovine rhodopsin. G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell and ...
G protein-coupled receptors (GPCRs) are a large family of integral membrane proteins that respond to a variety of extracellular stimuli. Each GPCR binds to and is activated by a specific ligand stimulus that ranges in size from small molecule catecholamines, lipids, or neurotransmitters to large protein hormones. [3]
At the cell surface, the binding of ligands such as hormones and neurotransmitters to a GPCR activates the receptor by causing a conformational change, which in turn activates the bound G protein on the intracellular-side of the membrane. The activated receptor promotes the exchange of bound GDP for GTP on the G protein alpha subunit.
Ligands connect to specific receptor proteins based on the shape of the active site of the protein. The receptor releases a messenger once the ligand has connected to the receptor. In biochemistry and pharmacology , receptors are chemical structures, composed of protein , that receive and transduce signals that may be integrated into biological ...
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene [5] and a G-protein-coupled receptor (GPCR). It is a light-sensitive receptor protein that triggers visual phototransduction in rod cells. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. [6]
The GPCR superfamily is the largest gene family in the human genome containing approximately 800 genes. [8] As the vertebrate superfamily can be phylogenetically grouped into five main families, the GRAFS classification system has been proposed, which includes the glutamate, rhodopsin, adhesion, Frizzled/Taste2, and secretin GPCR families.
The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormone, neuropeptide, neurotransmitter, and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins.
When ligands bind a GPCR, the GPCR acquires GEF (guanine nucleotide exchange factor) ability, which activates the G-protein by exchanging the GDP on the alpha subunit to GTP. The binding of GTP to the alpha subunit results in a structural change and its dissociation from the rest of the G-protein.