ArticleEuropean biophysics journal : EBJ2023
Analysis of residue-residue interactions in the structures of ASIC1a suggests possible gating mechanisms.
Article in European biophysics journal : EBJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- A proton-gated channel identified in the centipede antenna.EMBO reports · 2025Article
- Structure and function of a broad-range thermal receptor in myriapods.Nature structural & molecular biology · 2025Article
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Authors and funding
2 authors.
Funding
Abstract
The gating mechanism of acid-sensitive ion channels (ASICs) remains unclear, despite the availability of atomic-scale structures in various functional states. The collapse of the acidic pocket and structural changes in the low-palm region are assumed to trigger activation. For the acidic pocket, protonation of some residues can minimize repulsion in the collapsed conformation. The relationship between low-palm rearrangements and gating is unknown. In this work, we performed a Monte Carlo energy optimization of known ASIC1a structures and determined the residue-residue interactions in different functional states. For rearrangements in the acidic pocket, our results are consistent with previously proposed mechanisms, although significant complexity was revealed for the residue-residue interactions. The data support the proposal of a gating mechanism in the low-palm region, in which residues E80 and E417 share a proton to activate the channel.
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36690863What Socratic holds
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