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Pubmed for Handhelds

PUBMED FOR HANDHELDS

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  • Title: Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels.
    Author: Kuldyushev NA, Mineev KS, Berkut AA, Peigneur S, Arseniev AS, Tytgat J, Grishin EV, Vassilevski AA.
    Journal: Proteins; 2018 Oct; 86(10):1117-1122. PubMed ID: 30007037.
    Abstract:
    Sodium channel alpha-toxins from scorpion venom (α-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 α-NaTx classified as an "α-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.
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