In:
The FEBS Journal, Wiley, Vol. 279, No. 8 ( 2012-04), p. 1495-1504
Abstract:
Scorpion toxins targeting voltage‐gated sodium (Na V ) channels are peptides that comprise 60–76 amino acid residues cross‐linked by four disulfide bridges. These toxins can be divided in two groups (α and β toxins), according to their binding properties and mode of action. The scorpion α‐toxin Ts2, previously described as a β‐toxin, was purified from the venom of Tityus serrulatus , the most dangerous Brazilian scorpion. In this study, seven mammalian Na V channel isoforms (rNa V 1.2, rNa V 1.3, rNa V 1.4, hNa V 1.5, mNa V 1.6, rNa V 1.7 and rNa V 1.8) and one insect Na V channel isoform (DmNa V 1) were used to investigate the subtype specificity and selectivity of Ts2. The electrophysiology assays showed that Ts2 inhibits rapid inactivation of Na V 1.2, Na V 1.3, Na V 1.5, Na V 1.6 and Na V 1.7, but does not affect Na V 1.4, Na V 1.8 or DmNa V 1. Interestingly, Ts2 significantly shifts the voltage dependence of activation of Na V 1.3 channels. The 3D structure of this toxin was modeled based on the high sequence identity (72%) shared with Ts1, another T. serrulatus toxin. The overall fold of the Ts2 model consists of three β‐strands and one α‐helix, and is arranged in a triangular shape forming a cysteine‐stabilized α‐helix/β‐sheet (CSαβ) motif. Database Model data are available in the PMDB under accession number PM0077533 .
Type of Medium:
Online Resource
ISSN:
1742-464X
,
1742-4658
DOI:
10.1111/ejb.2012.279.issue-8
DOI:
10.1111/j.1742-4658.2012.08545.x
Language:
English
Publisher:
Wiley
Publication Date:
2012
detail.hit.zdb_id:
2172518-4
SSG:
12
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