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Article

Natural mutations change the affinity of μ-theraphotoxin-Hhn2a to voltage-gated sodium channels.

Toxicon : official journal of the International Society on Toxinology - 1 Jan 2015

Zhang Fan, Liu Yu, Zhang Changxin, Li Jing, Yang Zuqin, Gong Xue, Gan Yunxiang, Chen Ping, Liu Zhonghua, Liang Songping

Abstract excerpt

μ-Theraphotoxin-Hhn2a (HNTX-III) isolated from the venom of the spider Ornithoctonus hainana is a selective antagonist of neuronal tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channels (VGSCs). Intriguingly, previous transcriptomic study revealed HNTX-III family consists of more than 15 precursors, in which the 20(th) and 24(th) residues of the mature sequences are variable. Try20 and Ser24 of HNTX-III are...

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PMID: 25447770
DOI: 10.1016/j.toxicon.2014.11.220

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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