ArticleeLife2020
Structural insights into human acid-sensing ion channel 1a inhibition by snake toxin mambalgin1.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
- Conformational plasticity of human acid-sensing ion channel 1a.Nature structural & molecular biology · 2026Article
- Structural basis for a central permeation pathway in the P2X1 receptor.Cell discovery · 2026Article
- PUFA modulation of ASIC3 involves both specific and lipid solvent-like interactions.bioRxiv : the preprint server for biology · 2026Article
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- Structure and function of a broad-range thermal receptor in myriapods.Nature structural & molecular biology · 2025Article
- Two Amino Acid Substitutions Improve the Pharmacological Profile of the Snake Venom Peptide Mambalgin.Toxins · 2025Article
- Article
- Voltage-clamp fluorometry for advancing mechanistic understanding of ion channel mechanisms with a focus on acid-sensing ion channels.Biochemical Society transactions · 2024Review
- Article
- Revealing molecular determinants governing mambalgin-3 pharmacology at acid-sensing ion channel 1 variants.Cellular and molecular life sciences : CMLS · 2024Article
- Identification of the modulatory CaOpen biology · 2024Article
- Molecular basis of proton-sensing by G protein-coupled receptors.bioRxiv : the preprint server for biology · 2024Article
- The small molecule activator S3969 stimulates the epithelial sodium channel by interacting with a specific binding pocket in the channel's β-subunit.The Journal of biological chemistry · 2024Article
- Epithelial NaComprehensive Physiology · 2024Review
- Photomodulation of the ASIC1a acidic pocket destabilizes the open state.Protein science : a publication of the Protein Society · 2023Article
- Molecular Basis for Mambalgin-2 Interaction with Heterotrimeric α-ENaC/ASIC1a/γ-ENaC Channels in Cancer Cells.Toxins · 2023Article
- Mechanosensitive Ion Channels: Their Physiological Importance and Potential Key Role in Cancer.International journal of molecular sciences · 2023Review
- AFTM: a database of transmembrane regions in the human proteome predicted by AlphaFold.Database : the journal of biological databases and curation · 2023Article
- Modulation of Slow Desensitization (Tachyphylaxis) of Acid-Sensing Ion Channel (ASIC)1a.Cellular and molecular neurobiology · 2023Article
- Analysis of residue-residue interactions in the structures of ASIC1a suggests possible gating mechanisms.European biophysics journal : EBJ · 2023Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Acid-sensing ion channels (ASICs) are proton-gated cation channels that are involved in diverse neuronal processes including pain sensing. The peptide toxin Mambalgin1 (Mamba1) from black mamba snake venom can reversibly inhibit the conductance of ASICs, causing an analgesic effect. However, the detailed mechanism by which Mamba1 inhibits ASIC1s, especially how Mamba1 binding to the extracellular domain affects the conformational changes of the transmembrane domain of ASICs remains elusive. Here, we present single-particle cryo-EM structures of human ASIC1a (hASIC1a) and the hASIC1a-Mamba1 complex at resolutions of 3.56 and 3.90 Å, respectively. The structures revealed the inhibited conformation of hASIC1a upon Mamba1 binding. The combination of the structural and physiological data indicates that Mamba1 preferentially binds hASIC1a in a closed state and reduces the proton sensitivity of the channel, representing a closed-state trapping mechanism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.