The class C G-protein-coupled receptors are a class of G-protein coupled receptors. Similar to other GPCRs, the molecular structure of family C GPCRs contains an N-terminal signal sequence, 7TM domains that are linked by three intracellular, three extracellular loops, and an intracellular C-terminal amino acid sequence.
The ECD of family C GPCRs has been found to be closely related to bacterial periplasmic amino acid binding proteins, which transport nutrients from the extracellular to the intracellular space in bacteria. On the other hand, the 7TM domain of family C GPCRs is phylogenetically related to rhodopsin-like (family A) GPCRs. Family C G-protein-coupled receptors are characterized by a large extracellular domain containing the orthosteric agonist binding site known as the "Venus Flytrap Module" because of the dynamics of their bifida structures and their activation mechanism. Many suitable biochemical and electrophysiological assay systems reveal the complexity of the interaction between orthosteric and allosteric ligands. Many allosteric class C GPCR modulators show in vivo efficacy in a variety of behavioral models of clinical indications.
Fig.1 Schematic representation of a family C GPCR protein. (Urwyler, 2011)
The class C G-protein-coupled receptors comprise various pheromone, vomeronasal, and taste receptors, the calcium-sensing receptor (CaSR), as well as gamma-amino-butyric acid (GABA) type B receptors and glutamate receptors. Here shows part of family C G-protein-coupled receptors in humans:
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