Exploring structural features of the interaction between the scorpion ToxinCnErg1 and ERG K+ channels
文献类型：期刊论文
| 作者 | Frenal, K; Xu, CQ; Wolff, N; Wecker, K; Gurrola, GB; Zhu, SY; Chi, CW; Possani, LD; Tytgat, J; Delepierre, M |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2004 |
| 卷号 | 56期号:2页码:367-375 |
| 关键词 | ERG channel ergtoxin evolutionary trace analysis NMR structure scorpion toxin |
| 通讯作者 | Tytgat, J (reprint author), Univ Louvain, Toxicol Lab, B-3000 Louvain, Belgium.,murield@pasteur.fr |
| 英文摘要 | The gamma-KTx-type scorpion toxins specific for K+ channels were found to interact with ERG channels on the turret region, while alpha-KTx3.2 Agitoxin-2 binds to the pore region of the Shaker K+ channel, and alpha-KTx5.3 BmP05 binds to the intermediate region of the small-conductance calcium-activated K-channel (SKCa). In order to explore the critical residues for gamma-KTx binding, we determined the NMR structure of native gamma-KTx1.1 (CnErg1), a 42 amino acid residues scorpion toxin isolated from the venom of the Mexican scorpion Centruroides noxius Hoffmann, and we used computational evolutionary trace (ET) analysis to predict possible structural and functional features of interacting surfaces. The H-1-NMR three-dimensional solution structure of native ergtoxin (CnErg1) was solved using a total of 452 distance constraints, 13 (3)J(NH-Halpha) and 10 hydrogen bonds. The structure is characterized by 2 segments of alpha-helices and a triple-stranded antiparallel beta-sheet stabilized by 4 disulfide bridges. The ET and structural analysis provided indication of the presence of two important amino acid residue clusters, one hydrophobic and the other hydrophilic, that should be involved in the surface contact between the toxin and the channel. Some features of the proposed interacting surface are discussed. (C) 2004 Wiley-Liss, Inc. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | EVOLUTIONARY TRACE ANALYSIS ; POTASSIUM CHANNEL ; FUNCTIONAL SITES ; BINDING-SITE ; TOXIN ; SPECTROSCOPY ; PROTEINS ; ERGTOXIN ; PEPTIDE ; CENTRUROIDES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000222403300017 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2033]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Frenal, K,Xu, CQ,Wolff, N,et al. Exploring structural features of the interaction between the scorpion ToxinCnErg1 and ERG K+ channels[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2004,56(2):367-375. |
| APA | Frenal, K.,Xu, CQ.,Wolff, N.,Wecker, K.,Gurrola, GB.,...&Delepierre, M.(2004).Exploring structural features of the interaction between the scorpion ToxinCnErg1 and ERG K+ channels.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,56(2),367-375. |
| MLA | Frenal, K,et al."Exploring structural features of the interaction between the scorpion ToxinCnErg1 and ERG K+ channels".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 56.2(2004):367-375. |
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