Structure, inhibition and regulation of two-pore channel TPC1 from Arabidopsis thaliana

The X-ray crystal structure of a two-pore channel from Arabidopsis thaliana is reported, revealing the mechanisms of ion permeation, inhibition channel activation, and location of regulatory sites and voltage-sensing domains. Characterization of the two-pore channel AtTPC1 The X-ray crystal structur...

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Veröffentlicht in:	Nature (London) 2016-03, Vol.531 (7593), p.258-264
Hauptverfasser:	Kintzer, Alexander F., Stroud, Robert M.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/535/1266 631/92/269 Allosteric Regulation - drug effects Arabidopsis - chemistry Arabidopsis Proteins - antagonists & inhibitors Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism Arabidopsis thaliana Binding Sites Calcium - metabolism Calcium - pharmacology Calcium Channels - chemistry Calcium Channels - metabolism Carbolines - metabolism Carbolines - pharmacology Crystal structure Crystallography, X-Ray Ebolavirus - drug effects Endosomes - drug effects Endosomes - metabolism Endosomes - virology Flowers & plants Humanities and Social Sciences Ion Channel Gating - drug effects Ion Transport - drug effects letter Membranes Models, Molecular multidisciplinary Mutagenesis Phosphorylation Physiological aspects Piperazines - metabolism Piperazines - pharmacology Plant proteins Protein Structure, Tertiary - drug effects Science
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