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- W1974548955 abstract "Acid-sensing ion channels (ASICs) detect extracellular protons produced during inflammation or ischemic injury and belong to the superfamily of degenerin/epithelial sodium channels. Here, we determine the cocrystal structure of chicken ASIC1a with MitTx, a pain-inducing toxin from the Texas coral snake, to define the structure of the open state of ASIC1a. In the MitTx-bound open state and in the previously determined low-pH desensitized state, TM2 is a discontinuous α helix in which the Gly-Ala-Ser selectivity filter adopts an extended, belt-like conformation, swapping the cytoplasmic one-third of TM2 with an adjacent subunit. Gly 443 residues of the selectivity filter provide a ring of three carbonyl oxygen atoms with a radius of ∼3.6 Å, presenting an energetic barrier for hydrated ions. The ASIC1a-MitTx complex illuminates the mechanism of MitTx action, defines the structure of the selectivity filter of voltage-independent, sodium-selective ion channels, and captures the open state of an ASIC." @default.
- W1974548955 created "2016-06-24" @default.
- W1974548955 creator A5008840086 @default.
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- W1974548955 date "2014-02-01" @default.
- W1974548955 modified "2023-10-15" @default.
- W1974548955 title "X-Ray Structure of Acid-Sensing Ion Channel 1–Snake Toxin Complex Reveals Open State of a Na+-Selective Channel" @default.
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- W1974548955 doi "https://doi.org/10.1016/j.cell.2014.01.011" @default.
- W1974548955 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4190031" @default.
- W1974548955 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24507937" @default.
- W1974548955 hasPublicationYear "2014" @default.
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