9MLV
Structure of acid-sensing ion channel 5 without calcium, closed
Summary for 9MLV
| Entry DOI | 10.2210/pdb9mlv/pdb |
| EMDB information | 48380 |
| Descriptor | Acid-sensing ion channel 5 (1 entity in total) |
| Functional Keywords | ion channel, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 172593.04 |
| Authors | |
| Primary citation | Freitas, M.M.,Gouaux, E. The bile acid-sensitive ion channel is gated by Ca 2+ -dependent conformational changes in the transmembrane domain. Nat Commun, 16:6746-6746, 2025 Cited by PubMed Abstract: The bile acid-sensitive ion channel (BASIC) is the least understood member of the mammalian epithelial Na channel/degenerin (ENaC/DEG) superfamily of ion channels, which are involved in a variety of physiological processes. While some members of this superfamily, including BASIC, are inhibited by extracellular Ca (Ca), the molecular mechanism underlying Ca modulation remains unclear. Here, by determining the structure of human BASIC (hBASIC) in the presence and absence of Ca using single-particle cryo-electron microscopy (cryo-EM), we reveal Ca-dependent conformational changes in the transmembrane domain and β-linkers. Electrophysiological experiments further show that a glutamate residue in the extracellular vestibule of the pore underpins the Ca-binding site, whose occupancy determines the conformation of the pore and therefore ion flow through the channel. These results reveal the molecular principles governing gating of BASIC and its regulation by Ca ions, demonstrating that Ca ions modulate BASIC function via changes in protein conformation rather than solely from a pore-block, as proposed for other members of this superfamily. PubMed: 40695804DOI: 10.1038/s41467-025-62038-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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