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Diverse binding poses of agonistic neurotoxins on human Na<sub>v</sub>1.6

This research article presents structural insights into the diverse binding poses of agonistic neurotoxins on the human voltage-gated sodium channel Na_v1.6. The study utilizes cryo-electron microscopy (cryo-EM) to determine the structures of Na_v1.6 in complex with three different neurotoxins: Cn2, ι-RXIA, and Pc1a. These findings contribute to understanding the molecular mechanisms underlying toxin-channel interactions, which could have implications for drug development targeting these channels.

Data availability

Data supporting the findings of this study are available within the Article and its Supplementary Information . The cryo-EM maps have been deposited in the EMDB under accession codes EMD-80133 (Na v 1.6–Cn2), EMD-80134 (Na v 1.6–ι-RXIA) and EMD-80135 (Na v 1.6–Pc1a). The coordinates have been deposited in the PDB under accession codes 25IH (Na v 1.6–Cn2), 25II (Na v 1.6–ι-RXIA) and 25IJ (Na v 1.6–Pc1a).  Source data are provided with this paper.

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Source document: Evolutionary context of venom in animals

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Nature NewsParty-alignedCenter11 days ago
Diverse binding poses of agonistic neurotoxins on human Na<sub>v</sub>1.6

This research article presents structural insights into the diverse binding poses of agonistic neurotoxins on the human voltage-gated sodium channel Na_v1.6. The study utilizes cryo-electron microscopy (cryo-EM) to determine the structures of Na_v1.6 in complex with three different neurotoxins: Cn2, ι-RXIA, and Pc1a. These findings contribute to understanding the molecular mechanisms underlying toxin-channel interactions, which could have implications for drug development targeting these channels.

Bias read (Center): The article focuses on scientific research related to neurotoxin binding to sodium channels. It does not present any political opinions, arguments, or framing that would indicate a particular ideological lean. The content is purely descriptive and technical, centered around biological and medical-sy

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