Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxin

Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxin

Venom toxins are invaluable tools for exploring the structure and mechanisms of ion channels. Here, we solve the structure of double-knot toxin (DkTx), a tarantula toxin that activates the heat-activated TRPV1 channel. We also provide improved structures of TRPV1 with and without the toxin bound, an...

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Bibliographic Details
Main Authors: Chanhyung Bae, Claudio Anselmi, Jeet Kalia, Andres Jara-Oseguera, Charles D Schwieters, Dmitriy Krepkiy, Chul Won Lee, Eun-Hee Kim, Jae Il Kim, José D Faraldo-Gómez, Kenton J Swartz
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2016-02-01
Series:eLife
Subjects:
capsaicin
thermosensing
membrane channel
membrane structure
protein-protein interactions in membranes
Online Access:https://elifesciences.org/articles/11273

Internet

https://elifesciences.org/articles/11273

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