Structure of MeuNaTxα‐1 toxin from scorpion venom highlights the importance of the nest motif. Issue 8 (24th March 2021)

• Record Type: Journal Article
• Authors: Mineev, Konstantin S.; Kuzmenkov, Alexey I.; Arseniev, Alexander S.; Vassilevski, Alexander A.
• Is Part Of: Proteins. Volume 89:Issue 8(2021)
• Page Start: 1055
• Page End: 1060
• Publication Date: 2021-03-24
• Subjects: ion channel -- neurotoxin -- protein motif -- voltage‐gated sodium channel; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.26074
• Languages: English
• ISSNs: 0887-3585

Abstract

Abstract: 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.