1pvz

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Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures

Overview

A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily, alpha-KTx 14), which is composed of 31 amino acid residues and purified, from the venom of the Chinese scorpion Buthus martensi Karsch, was, characterized using whole-cell patch-clamp recording in rat hippocampal, neurons. The three dimensional structure of BmKK2 was determined with, two-dimensional NMR spectroscopy and molecular modelling techniques. In, solution this toxin adopted a common alpha/beta-motif, but showed distinct, local conformation in the loop between alpha-helix and beta-sheet in, comparison with typical short-chain scorpion toxins (e.g., CTX and NTX)., Also, the alpha helix is shorter and the beta-sheet element is smaller, (each strand consisted only two residues). The unusual structural feature, of BmKK2 was attributed to the shorter loop between the alpha-helix and, beta-sheet and the presence of two consecutive Pro residues at position 21, and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and, BmKK2/rSK2 channel complexes were simulated with docking calculations. The, results demonstrated the existence of a alpha-mode binding between the, toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited, favorable contacts both in electrostatic and hydrophobic, including a, network of five hydrogen bonds and bigger interface containing seven pairs, of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3, channel complex, containing only three pairs of inter-residue, interactions, exhibited poor contacts and smaller interface. The results, well explained its lower activity towards Kv channel, and predicted that, it may prefer a type of SK channel with a narrower entryway as its, specific receptor.

About this Structure

1PVZ is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.

Reference

Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch., Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H, Proteins. 2004 Jun 1;55(4):835-45. PMID:15146482

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