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3S3W

Structure of chicken acid-sensing ion channel 1 at 2.6 a resolution and ph 7.5

Summary for 3S3W
Entry DOI10.2210/pdb3s3w/pdb
DescriptorAmiloride-sensitive cation channel 2, neuronal, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsacid-sensing, ion channel, cell membrane, glycoprotein, ion transport, membrane, sodium transport, transmembrane, transport, transport protein, membrane glycoprotein, sodium channel, membrane protein
Biological sourceGallus gallus (bantam,chickens)
Total number of polymer chains3
Total formula weight159911.73
Authors
Dawson, R.J.P.,Benz, J.,Stohler, P.,Tetaz, T.,Joseph, C.,Huber, S.,Schmid, G.,Huegin, D.,Pflimlin, P.,Trube, G.,Rudolph, M.G.,Hennig, M.,Ruf, A. (deposition date: 2011-05-18, release date: 2012-05-23, Last modification date: 2024-11-06)
Primary citationDawson, R.J.,Benz, J.,Stohler, P.,Tetaz, T.,Joseph, C.,Huber, S.,Schmid, G.,Hugin, D.,Pflimlin, P.,Trube, G.,Rudolph, M.G.,Hennig, M.,Ruf, A.
Structure of the Acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1.
Nat Commun, 3:936-936, 2012
Cited by
PubMed Abstract: Venom-derived peptide toxins can modify the gating characteristics of excitatory channels in neurons. How they bind and interfere with the flow of ions without directly blocking the ion permeation pathway remains elusive. Here we report the crystal structure of the trimeric chicken Acid-sensing ion channel 1 in complex with the highly selective gating modifier Psalmotoxin 1 at 3.0 Å resolution. The structure reveals the molecular interactions of three toxin molecules binding at the proton-sensitive acidic pockets of Acid-sensing ion channel 1 and electron density consistent with a cation trapped in the central vestibule above the ion pathway. A hydrophobic patch and a basic cluster are the key structural elements of Psalmotoxin 1 binding, locking two separate regulatory regions in their relative, desensitized-like arrangement. Our results provide a general concept for gating modifier toxin binding suggesting that both surface motifs are required to modify the gating characteristics of an ion channel.
PubMed: 22760635
DOI: 10.1038/ncomms1917
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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数据于2025-06-18公开中

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