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Structure of MeuNaTxα‐1 toxin from scorpion venom highlights the importance of the nest motif
Author(s) -
Mineev Konstantin S.,
Kuzmenkov Alexey I.,
Arseniev Alexander S.,
Vassilevski Alexander A.
Publication year - 2021
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.26074
Subject(s) - venom , scorpion , scorpion toxin , buthidae , toxin , scorpion venoms , biology , computational biology , evolutionary biology , ecology , biochemistry
Old world scorpions produce an abundance of toxins called α‐NaTx, which interfere with the fast inactivation of voltage‐gated sodium channels. Their selectivity to channels of mammals or insects depends on a part of toxin named the specificity module. We report here the spatial structure of a major and broadly active toxin MeuNaTxα‐1 from the venom of Mesobuthus eupeus . Notably, its specificity module is markedly different from other α‐NaTx with known 3D structure. Close inspection shows that its conformation is a result of an interplay between protein motifs such as the nest and niche, which eventually shape α‐NaTx structural diversity.

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