Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2

Article ID	Journal	Published Year	Pages	File Type
8298018	Biochemical and Biophysical Research Communications	2011	7 Pages	PDF

Abstract

âº Channelrhodopsin 2 is a light-activated cation channel widely used in neurobiology. âº We show its transmembrane segment 2 to be crucial for ion conductance. âº Transmembrane segment 2 forms a hydrophilic amphipathic helix. âº Glutamate 90 located within this helix determines cation flux and selectivity.

Keywords

Channelrhodopsin 2 Voltage-clamp recording amphipathic helix Ion selectivity Photocurrent Cation channel

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

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Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2

Authors

Karelia Ruffert, Bettina Himmel, Deepti Lall, Christian Bamann, Ernst Bamberg, Heinrich Betz, Volker Eulenburg,