Structural basis for the modulation of voltage-gated sodium channels by animal toxins

Huaizong Shen, Zhangqiang Li, Yan Jiang, Xiaojing Pan, Jianping Wu, Ben Cristofori-Armstrong, Jennifer J. Smith, Yanni K.Y. Chin, Jianlin Lei, Qiang Zhou, Glenn F. King, Nieng Yan

Research output: Contribution to journalArticleResearchpeer-review

177 Citations (Scopus)

Abstract

Animal toxins that modulate the activity of voltage-gated sodium (Nav) channels are broadly divided into two categories-pore blockers and gating modifiers.The pore blockers tetrodotoxin (TTX) and saxitoxin (STX) are responsible for puffer fish and shellfish poisoning in humans, respectively. Here, we present structures of the insect Nav channel NavPaS bound to a gatingmodifier toxin Dc1a at 2.8 angstrom-resolution and in the presence of TTXor STX at 2.6-Å and 3.2-Å resolution, respectively. Dc1a inserts into the cleft between VSDII and the pore of NavPaS, making key contacts with both domains. The structures with bound TTX or STX reveal the molecular details for the specific blockade of Na+ access to the selectivity filter from the extracellular side by these guanidinium toxins. The structures shed light on structure-based development of Nav channel drugs.

Original languageEnglish
Article numbereaau2596
Number of pages8
JournalScience
Volume362
Issue number6412
DOIs
Publication statusPublished - 19 Oct 2018
Externally publishedYes

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