Structure of the Acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-01

AUTHORS

Roger J.P. Dawson, Jörg Benz, Peter Stohler, Tim Tetaz, Catherine Joseph, Sylwia Huber, Georg Schmid, Daniela Hügin, Pascal Pflimlin, Gerd Trube, Markus G. Rudolph, Michael Hennig, Armin Ruf

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. More... »

PAGES

936

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms1917

DOI

http://dx.doi.org/10.1038/ncomms1917

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036676767

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22760635


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