1WM7

Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures

1WM7 の概要

• エントリーDOI: 10.2210/pdb1wm7/pdb
• 関連するPDBエントリー: 1ACW 1DU9 1PNH 1SCY
• 分子名称: Neurotoxin BmP01 (1 entity in total)
• 機能のキーワード: alpha/beta scaffold, toxin
• 由来する生物種: Mesobuthus martensii (Chinese scorpion)
• 細胞内の位置: Secreted: Q9U8D2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3188.57

構造登録者

Wu, G.,Li, Y.,Wei, D.,He, F.,Jiang, S.,Hu, G.,Wu, H.,Chen, X. (登録日: 2004-07-05, 公開日: 2004-07-27, 最終更新日: 2024-11-13)

主引用文献

Wu, G.,Li, Y.,Wei, D.,He, F.,Jiang, S.,Hu, G.,Wu, H.
Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch
Biochem.Biophys.Res.Commun., 276:1148-1154, 2000

PubMed Abstract: From the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem. 245, 457-464). It was shown to reduce 33% outward K(+) channel (hippocampal neurons) currents at 10 microM. The solution structure of BmP01 was determined by 2D (1)H NMR spectroscopy. The NOEs, coupling constants, and H-D exchange obtained from NMR spectroscopy were used in structural calculations. The conformation of BmP01 is composed of a short alpha-helix (Cys 3-Thr 12) and a two-stranded antiparallel beta-sheet (Ala 15-Asp 20 and Lys 23-Pro 28). There are three disulfide bridges (Cys 3-Cys 19, Cys 6-Cys 24 and Cys 10-Cys 26) connecting the alpha-helix and beta-sheet. Asp 20 to Lys 23 form a type II turn linking the two strands. Structural and electrostatic potential comparison between BmP01 and its analogues are also presented.

PubMed: 11027603
DOI: 10.1006/bbrc.2000.3435

実験手法

SOLUTION NMR