6THI

Solution structure of MeuNaTxalpha-1 toxin from Mesobuthus Eupeus

Summary for 6THI

• Entry DOI: 10.2210/pdb6thi/pdb
• NMR Information: BMRB: 34453
• Descriptor: Sodium channel neurotoxin MeuNaTxalpha-1 (1 entity in total)
• Functional Keywords: toxin, alpha-toxin, sodium channel blocker
• Biological source: Mesobuthus eupeus (Lesser Asian scorpion)
• Total number of polymer chains: 1
• Total formula weight: 7196.15

Authors

Mineev, K.S.,Kuzmenkov, A.I.,Khusainov, G.A.,Arseniev, A.S.,Vassilevski, A.A. (deposition date: 2019-11-20, release date: 2020-12-02, Last modification date: 2024-10-16)

Primary citation

Mineev, K.S.,Kuzmenkov, A.I.,Arseniev, A.S.,Vassilevski, A.A.
Structure of MeuNaTx alpha-1 toxin from scorpion venom highlights the importance of the nest motif.
Proteins, 2021

PubMed 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.

PubMed: 33713480
DOI: 10.1002/prot.26074

Experimental method

SOLUTION NMR