Neurotransmitter-gated ion-channel, conserved site
Short name | Neurotransmitter_ion_chnl_CS |
Description
* Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits
* Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits
* Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known
* Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7)
* Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate)
References
1.Structural features of the ligand-binding domain of the serotonin 5HT3 receptor. Yan D, Schulte MK, Bloom KE, White MM. J. Biol. Chem. 274, 5537-41, (1999). View articlePMID: 10026168
2.Structure and gating of the glutamate receptor ion channel. Wollmuth LP, Sobolevsky AI. Trends Neurosci. 27, 321-8, (2004). View articlePMID: 15165736
3.Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor. Wagner K, Edson K, Heginbotham L, Post M, Huganir RL, Czernik AJ. J. Biol. Chem. 266, 23784-9, (1991). View articlePMID: 1721053
4.Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing. Kofuji P, Wang JB, Moss SJ, Huganir RL, Burt DR. J. Neurochem. 56, 713-5, (1991). View articlePMID: 1846404
5.Molecular structure and function of the glycine receptor chloride channel. Lynch JW. Physiol. Rev. 84, 1051-95, (2004). PMID: 15383648
6.GABA(A) receptors: Subtypes provide diversity of function and pharmacology. Olsen RW, Sieghart W. Neuropharmacology (2008). PMID: 18760291
7.Assembly and trafficking of nicotinic acetylcholine receptors (Review). Millar NS, Harkness PC. Mol. Membr. Biol. 25, 279-92, (2008). View articlePMID: 18446614
Cross References
ENZYME
Contributing Member Database Entry
- PROSITE patterns:PS00236