AI Article Synopsis
- Scorpion α-toxins (α-NaTx) are small proteins that inhibit the inactivation of voltage-gated sodium channels and have a specific structure for binding sodium.
- The study focuses on the structure of the Lqq4 toxin, revealing it exists in multiple stable forms due to different configurations of peptide bonds, specifically V56-P57 and C17-G18.
- These findings suggest that the natural range of shapes (conformational space) for α-NaTx proteins is broader than previously thought.
Article Abstract
Scorpion α-toxins (α-NaTx) inhibiting the inactivation of voltage-gated sodium channels (Na ) are a well-studied family of small proteins. We previously showed that the structure of α-NaTx specificity module responsible for selective Na binding is governed by an interplay between the nest and niche protein motifs. Here, we report the solution structure of the toxin Lqq4 from the venom of the scorpion Leiurus quinquestriatus. Unexpectedly, we find that this toxin presents an ensemble of long-lived structurally distinct states. We unequivocally assign these states to the alternative configurations (cis-trans isomers) of two peptide bonds: V56-P57 and C17-G18; neither of the cis isomers has been described in α-NaTx so far. We argue that the native conformational space of α-NaTx is wider than assumed previously.
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| http://dx.doi.org/10.1002/1873-3468.14705 | DOI Listing |
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