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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...
Αποθηκεύτηκε σε:
| Τόπος έκδοσης: | eLife |
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| Κύριοι συγγραφείς: | , , , , , , , , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
eLife Sciences Publications, Ltd
2016
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| Θέματα: | |
| Διαθέσιμο Online: | 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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