6thi | pdb_00006thi

Solution structure of MeuNaTxalpha-1 toxin from Mesobuthus Eupeus

spinqualitylabelsall models 6thi, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6thi is a 1 chain structure with sequence from Buthus eupeus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SCXN1_MESEU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin inhibits inactivation of Nav1.6/SCN8A (EC(50)=3.1 uM) and drosophila DmNav1 (EC(50)=1.17 uM) (PubMed:21969612, Ref.2). The toxin (1 uM) does not significantly shift the midpoint of activation at the two channels, but induces a significant depolarizing shift in the V(1/2) of inactivation of the channels (PubMed:21969612). [PROSITE-ProRule:PRU01210] Publication Abstract from PubMed Old world scorpions produce an abundance of toxins called alpha-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 MeuNaTxalpha-1 from the venom of Mesobuthus eupeus. Notably, its specificity module is markedly different from other alpha-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 alpha-NaTx structural diversity. Structure of MeuNaTxalpha-1 toxin from scorpion venom highlights the importance of the nest motif.,Mineev KS, Kuzmenkov AI, Arseniev AS, Vassilevski AA Proteins. 2021 Mar 13. doi: 10.1002/prot.26074. PMID:33713480 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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