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...
Main Authors: | , , , , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2016-02-01
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Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/11273 |