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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Detalles Bibliográficos
Publicado en:eLife
Autores principales: Bae, Chanhyung, Anselmi, Claudio, Kalia, Jeet, Jara-Oseguera, Andres, Schwieters, Charles D, Krepkiy, Dmitriy, Won Lee, Chul, Kim, Eun-Hee, Kim, Jae Il, Faraldo-Gómez, José D, Swartz, Kenton J
Formato: Artigo
Lenguaje:Inglês
Publicado: eLife Sciences Publications, Ltd 2016
Materias:
Biophysics and Structural Biology
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4764579/
https://ncbi.nlm.nih.gov/pubmed/26880553
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.11273
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