Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels.
Proteins
; 86(10): 1117-1122, 2018 10.
Article
em En
| MEDLINE
| ID: mdl-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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MEDLINE
Assunto principal:
Arginina
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Venenos de Escorpião
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Escorpiões
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Proteínas de Artrópodes
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Neurotoxinas
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article