| Name | TM3 |
|---|---|
| Synonyms | Alpha tropomyosin 3; TRK; NEM 1; NEM1; OK/SW cl.5; TM 5; TM3; TM30… |
| Name | strychnine |
|---|---|
| CAS | strychnidin-10-one |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19959465 | Melzer N, Villmann C, Becker K, Harvey K, Harvey RJ, Vogel N, Kluck CJ, Kneussel M, Becker CM: Multifunctional basic motif in the glycine receptor intracellular domain induces subunit-specific sorting. J Biol Chem. 2010 Feb 5;285(6):3730-9. Epub 2009 Dec 3. The strychnine-sensitive glycine receptor (GlyR) is a ligand-gated ion channel that mediates fast synaptic inhibition in the vertebrate central nervous system. Each subunit contains an extracellular ligand binding domain, four transmembrane domains (TM), and an intracellular domain, formed by the loop connecting TM3 and TM4 (TM3-4 loop). |
4(0,0,0,4) | Details |
| 15287902 | Lobo IA, Trudell JR, Harris RA: Cross-linking of glycine receptor transmembrane segments two and three alters coupling of ligand binding with channel opening. J Neurochem. 2004 Aug;90(4):962-9. We tested whether two amino acids in TM2 (S267) and TM3 (A288), known to be critical for and volatile anesthetic action, could cross-link by mutating both to cysteines and expressing the receptors in Xenopus laevis oocytes. In contrast with the wild-type receptor and single mutants, the S267C/A288C double mutant displayed unusual responses, including a tonic leak activity that was closed by strychnine and a run-down of the response upon repeated applications of |
2(0,0,0,2) | Details |
| 14593111 | Breitinger U, Breitinger HG, Bauer F, Fahmy K, Glockenhammer D, Becker CM: Conserved high affinity ligand binding and membrane association in the native and refolded extracellular domain of the human glycine receptor alpha1-subunit. J Biol Chem. 2004 Jan 16;279(3):1627-36. Epub 2003 Oct 30. The strychnine-sensitive glycine receptor (GlyR) is a ligand-gated chloride channel composed of ligand binding alpha- and gephyrin anchoring beta-subunits. To identify the secondary and quaternary structures of extramembraneous receptor domains, the N-terminal extracellular domain (alpha1-(1-219)) and the large intracellular TM3-4 loop (alpha1-(309-392)) of the human GlyR alpha1-subunit were individually expressed in HEK293 cells and in Escherichia coli. |
1(0,0,0,1) | Details |