Structural highlights
7usx is a 6 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | Electron Microscopy, Resolution 3.09Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
TMC1_CAEEL Pore-forming subunit of the mechanotransducer (MET) non-selective cation channel complex (PubMed:36224384). The MET complex is composed of symmetric dimeric MET channels, each channel comprising two copies of pore-forming ion-conducting transmembrane TMC subunits and auxiliary proteins including the transmembrane inner ear protein/tmie, the calcium-binding protein/calm-1 and arrestin domain protein arrd-6 (PubMed:36224384). Sodium ions are the most permeable, whereas calcium and potassium have lower indices (PubMed:23364694). Sodium-sensor ion channel that acts specifically in salt taste chemosensation. Required for salt-evoked neuronal activity and behavioral avoidance of high concentrations of NaCl.[1] [2]
References
- ↑ Chatzigeorgiou M, Bang S, Hwang SW, Schafer WR. tmc-1 encodes a sodium-sensitive channel required for salt chemosensation in C. elegans. Nature. 2013 Feb 7;494(7435):95-99. doi: 10.1038/nature11845. Epub 2013 Jan 30. PMID:23364694 doi:http://dx.doi.org/10.1038/nature11845
- ↑ Jeong H, Clark S, Goehring A, Dehghani-Ghahnaviyeh S, Rasouli A, Tajkhorshid E, Gouaux E. Structures of the TMC-1 complex illuminate mechanosensory transduction. Nature. 2022 Oct;610(7933):796-803. PMID:36224384 doi:10.1038/s41586-022-05314-8
