2BMT

SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES

2BMT の概要

• エントリーDOI: 10.2210/pdb2bmt/pdb
• NMR情報: BMRB: 4191
• 分子名称: TOXIN BMTX2 (1 entity in total)
• 機能のキーワード: scorpion, neurotoxin, large conductance potassium channel, voltage gated potassium channel, buthus martensii
• 由来する生物種: Mesobuthus martensii (Chinese scorpion)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4191.90

構造登録者

Blanc, E.,Romi-Lebrun, R.,Bornet, O.,Nakajima, T.,Darbon, H. (登録日: 1998-06-16, 公開日: 1999-01-13, 最終更新日: 2024-10-23)

主引用文献

Blanc, E.,Romi-Lebrun, R.,Bornet, O.,Nakajima, T.,Darbon, H.
Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels.
Biochemistry, 37:12412-12418, 1998

PubMed Abstract: The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface.

PubMed: 9730813
DOI: 10.1021/bi9809371

実験手法

SOLUTION NMR