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• W2034352765 abstract "Acid-sensing ion channels are proton-activated, sodium-selective channels composed of three subunits, and are members of the superfamily of epithelial sodium channels, mechanosensitive and FMRF-amide peptide-gated ion channels. These ubiquitous eukaryotic ion channels have essential roles in biological activities as diverse as sodium homeostasis, taste and pain. Despite their crucial roles in biology and their unusual trimeric subunit stoichiometry, there is little knowledge of the structural and chemical principles underlying their ion channel architecture and ion-binding sites. Here we present the structure of a functional acid-sensing ion channel in a desensitized state at 3 Å resolution, the location and composition of the ∼8 Å ‘thick’ desensitization gate, and the trigonal antiprism coordination of caesium ions bound in the extracellular vestibule. Comparison of the acid-sensing ion channel structure with the ATP-gated P2X4 receptor reveals similarity in pore architecture and aqueous vestibules, suggesting that there are unanticipated yet common structural and mechanistic principles. P2X receptors are ATP-gated non-selective cation channels involved in nociception and inflammatory responses, whose structures were unknown. Kawate et al. now present the crystal structure of the zebrafish P2X4 receptor in a closed state. The trimeric structure reveals some of the molecular underpinnings of ligand-binding, cation entry and channel gating. A related paper presents the structure of chicken acid-sensing ion channel 1 (ASIC1) in a desensitized state. Like P2X receptors, ASICs are trimeric, but they belong to an entirely different family of ion channels. The structure determination of ASIC1 shows how ion permeation and desensitization may occur, and comparison of ASIC and P2X structures suggests that these functionally distinct channels employ similar mechanistic principles. Like P2X receptors, acid-sensing ion channels are trimeric in structure; however, they belong to an entirely different family. Here, the structure of an acid-sensing ion channel is presented and compared to the structure of P2X4, suggesting that these functionally distinct channels use similar mechanistic principles." @default.
• W2034352765 created "2016-06-24" @default.
• W2034352765 creator A5032551960 @default.
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• W2034352765 date "2009-07-01" @default.
• W2034352765 modified "2023-10-15" @default.
• W2034352765 title "Pore architecture and ion sites in acid-sensing ion channels and P2X receptors" @default.
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• W2034352765 doi "https://doi.org/10.1038/nature08218" @default.
• W2034352765 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2845979" @default.
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