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• W2051237359 abstract "Acid-sensing ion channels (ASICs) are voltage-independent, amiloride-sensitive channels involved in diverse physiological processes ranging from nociception to taste. Despite the importance of ASICs in physiology, we know little about the mechanism of channel activation. Here we show that psalmotoxin activates non-selective and Na+-selective currents in chicken ASIC1a at pH 7.25 and 5.5, respectively. Crystal structures of ASIC1a–psalmotoxin complexes map the toxin binding site to the extracellular domain and show how toxin binding triggers an expansion of the extracellular vestibule and stabilization of the open channel pore. At pH 7.25 the pore is approximately 10 Å in diameter, whereas at pH 5.5 the pore is largely hydrophobic and elliptical in cross-section with dimensions of approximately 5 by 7 Å, consistent with a barrier mechanism for ion selectivity. These studies define mechanisms for activation of ASICs, illuminate the basis for dynamic ion selectivity and provide the blueprints for new therapeutic agents. Acid-sensing ion channels (ASICs) are voltage-independent ion channels that participate in a broad range of biological processes, including nociception and mechanosensation; here X-ray crystal structures of the complexes of chicken ASIC1a with psalmotoxin, a peptide toxin from tarantula, indicate that toxin binding triggers an expansion of the extracellular vestibule and stabilization of the open channel pore. Acid-sensing ion channels (ASICs) are members of the epithelial sodium channel/degenerin (ENaC/DEG) superfamily of voltage-independent ion channels. ENaCs, including ASICs, participate in a broad range of biological processes, such as nociception, mechanosensation and regulation of sodium-ion homeostasis. Here, Isabelle Baconguis and Eric Gouaux show that psalmotoxin, a peptide toxin from the tarantula, activates nonselective and sodium-selective currents in chicken ASIC1a. X-ray crystal structures of the chicken ASIC1a–psalmotoxin complexes indicate that toxin binding triggers an expansion of the extracellular vestibule and stabilization of the open channel pore. This view of an important type of ion channel in an open conformation is of relevance to the design of open-channel blockers that might have therapeutic promise for the treatment of pain." @default.
• W2051237359 created "2016-06-24" @default.
• W2051237359 creator A5085520710 @default.
• W2051237359 creator A5088125571 @default.
• W2051237359 date "2012-07-29" @default.
• W2051237359 modified "2023-09-27" @default.
• W2051237359 title "Structural plasticity and dynamic selectivity of acid-sensing ion channel–spider toxin complexes" @default.
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• W2051237359 doi "https://doi.org/10.1038/nature11375" @default.
• W2051237359 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3725952" @default.
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