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学科主题: 生命有机化学
题名: The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx
其他题名: α-KTx 16亚家族钾通道堵塞肽BmTx3B的溶液结构
作者: WANG YUEFENG ; Chen X(陈翔) ; Zhang NX(张乃霞) ; Wu G(吴宫) ; Wu HM(吴厚铭)
通讯作者: 吴厚铭
刊名: Proteins
发表日期: 2005-01-01
卷: 58, 期:2, 页:489-497
收录类别: SCI
部门归属: 上海有机所
英文摘要: This article reports the solution structure of BmTx3B (alpha-KTx16.2), a potassium channel blocker belonging to the subfamily alpha-KTx16, purified from the venom of the Chinese scorpion Buthus martensi Karsch. In solution, BmTx3B assumes a typical CSalphabeta motif, with an alpha-helix connected to a triple-stranded P-sheet by 3 disulfide bridges, which belongs to the first structural group of short-chain scorpion toxins. On the other hand, BmTx3B is quite different from other toxins (such as ChTx and AgTx2) of this group in terms of the electrostatic and hydrophobic surface distribution. The functional surface (beta-face) of the molecule is characterized by less basic residues (only 2: Lys28 and Arg35) and extra aromatic residues (Phe1, Phe9, Trp15, and Tyr37). The peptide shows a great preference for the Kca1.1 channel over the Kv channel (about a 10(3)-fold difference). The model of BmTx3B/Kca1.1 channel complex generated by docking and dynamic simulation reveals that the stable binding between the BmTx3B and Kca1.1 channel is favored by a number of aromatic pi-pi stacking interactions. The influences of these structural features on the kinetic behavior of the toxin binding to Kca1.1 channel are also discussed. (C) 2004 Wiley-Liss, Inc.
语种: 英语
相关网址: 查看原文
内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/17365
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
WANG YUEFENG,Chen X,Zhang NX,et al. The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx[J]. Proteins,2005,58(2):489-497.
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