The Cys-loop ligand-gated ion channel superfamily is composed of nicotinic acetylcholine, GABAA, GABAA-ρ, glycine and 5-HT3 receptors that are composed of five protein subunits which form a pentameric arrangement around a central pore. There are usually 2 alpha subunits and 3 other beta, gamma or delta subunits (some consist of 5 alpha subunits). Cys-loop receptors possess a characteristic loop formed by a disulfide bond between two cysteine (Cys) residues 13 highly conserved amino acids apart near the N-terminal extracellular domain of the alpha subunit.
All subunits consist of a conserved extracellular large N-terminal domain; three highly conserved transmembrane domains; a cytoplasmic loop of variable size and amino acid sequence; and a fourth transmembrane domain with a relatively short and variable extracellular C terminal. All alpha subunits have a characteristic cys-cys pair in the N-terminal extracellular domain, this is shown to be essential for agonist binding. The neurotransmitters bind at the interface between subunits in the extracellular domain.
Each subunit contains 4 membrane-spanning alpha helixes (M1, M2, M3, M4), the pore is primarily formed by M2 of the two alpha subunits.
The M3-M4 linker is the intracellular domain that binds the cytoskeleton.
References
- Sine S, Engel A (2006). "Recent advances in Cys-loop receptor structure and function.". Nature 440 (7083): 448–55. doi:. PMID 16554804.
- Albuquerque et al (2009). "Mammalian Nicotinic Acetylcholine Receptors: from Structure to Function". Physiol Rev (89): 73-120. doi:.
See also
External links
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