Structural highlights
Function
[SCX9_MESEU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Has paralytic activity in mice.
Publication Abstract from PubMed
Sodium channel alpha-toxins from scorpion venom (alpha-NaTx) inhibit the inactivation of voltage-gated sodium channels. We used solution NMR to investigate the structure of BeM9 toxin from Mesobuthus eupeus scorpion, a prototype alpha-NaTx classified as an "alpha-like" toxin due to its wide spectrum of activity on insect and mammalian channels. We identified a new motif that we named "arginine hand", whereby arginine side chain forms several hydrogen bonds with main chain atoms. The arginine hand was found in the "specificity module", a part of the molecule that dictates toxin selectivity; and just single arginine-to-lysine point mutation drastically changed BeM9 selectivity profile. This article is protected by copyright. All rights reserved.
Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels.,Kuldyushev NA, Mineev KS, Berkut AA, Peigneur S, Arseniev AS, Tytgat J, Grishin EV, Vassilevski AA Proteins. 2018 Jul 14. doi: 10.1002/prot.25583. PMID:30007037[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuldyushev NA, Mineev KS, Berkut AA, Peigneur S, Arseniev AS, Tytgat J, Grishin EV, Vassilevski AA. Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels. Proteins. 2018 Jul 14. doi: 10.1002/prot.25583. PMID:30007037 doi:http://dx.doi.org/10.1002/prot.25583
