- Cys-loop receptors
-
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 that 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 formed primarily by M2 of the two alpha subunits.
The M3-M4 linker is the intracellular domain that binds the cytoskeleton.
See also
- Ion channel
- Nicotinic agonists
- Receptor (biochemistry)
References
- Sine S, Engel A (2006). "Recent advances in Cys-loop receptor structure and function.". Nature 440 (7083): 448–55. doi:10.1038/nature04708. PMID 16554804.
- Albuquerque et al. (2009). "Mammalian Nicotinic Acetylcholine Receptors: From Structure to Function". Physiol Rev 89 (1): 73–120. doi:10.1152/physrev.00015.2008. PMC 2713585. PMID 19126755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2713585.
External links
Ion channel, cell surface receptor: ligand-gated ion channels Cys-loop receptors monomers: α1 · α2 · α3 · α4 · α5 · α6 · α7 · α9 · α10 · β1 · β2 · β3 · β4 · δ · ε
pentamers: (α3)2(β4)3 · (α4)2(β2)3 · (α7)5 · (α1)2(β4)3 - Ganglion type · (α1)2β1δε - Muscle typeZincZinc-activatedIonotropic glutamates Ligand-gated onlyVoltage- and ligand-gated‘Orphan’ATP-gated channels This transmembrane receptor-related article is a stub. You can help Wikipedia by expanding it.