Unusual binding mode of scorpion toxin BmKTX onto potassium channels relies on its distribution of acidic residues
Unusual binding mode of scorpion toxin BmKTX onto potassium channels relies on its distribution of acidic residues
复制标题
蝎毒素 BmKTX 与钾通道的不寻常结合模式依赖于其酸性残基的分布
DOI：
10.1016/j.bbrc.2014.03.101
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发表时间：
2014-04-25
影响因子：
3.1
通讯作者：
Wu, Yingliang
中科院分区：
文献类型：
--
作者：
Chen, Zongyun;Hu, Youtian;Wu, Yingliang
除了经典的蝎子毒素-钾通道结合模式外，新的模式尚不清楚。在这里，我们报道了一种新的天然毒素BmKTX与K(v)1.3通道的结合模式。结合实验和计算数据表明，BmKTX-D33H模拟物使用经典的反平行β -sheet结构域作为通道相互作用界面，并使用保守的通道孔阻塞Lys（26）。然而，野生型BmKTX被发现使用Arg（23）而不是Lys26作为新的孔阻断残基，并且主要采用α -螺旋结构域和反平行β -sheet结构域之间的turn motif来识别K(v)1.3通道。综上所述，这些发现不仅揭示了蝎子毒素-钾通道相互作用模式的多样性，而且突出了毒素酸性残基在介导多种毒素-钾通道结合模式中的功能作用。(C) 2014爱思唯尔公司版权所有。
Besides classical scorpion toxin-potassium channel binding modes, novel modes remain unknown. Here, we report a novel binding mode of native toxin BmKTX towards K(v)1.3 channel. The combined experimental and computational data indicated that BmKTX-D33H analog used the classical anti-parallel beta-sheet domain as the channel-interacting interface together with the conserved channel pore-blocking Lys(26). However, the wild-type BmKTX was found to use Arg(23) rather than Lys26 as the new pore-blocking residue, and mainly adopt the turn motif between the alpha-helix and antiparallel beta-sheet domains to recognize K(v)1.3 channel. Together, these findings not only reveal that scorpion toxin-potassium channel interaction modes are more diverse than thought, but also highlight the functional role of toxin acidic residues in mediating diverse toxin-potassium channel binding modes. (C) 2014 Elsevier Inc. All rights reserved.