Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.
Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.
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DOI：
10.1038/srep21759
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发表时间：
2016-02-22
影响因子：
4.6
通讯作者：
Dempsey CE
中科院分区：
文献类型：
--
作者：
Armstrong CT;Mason PE;Anderson JL;Dempsey CE
电压敏感离子通道和酶的电压敏感区域(VSD)中的门控电荷由精氨酸侧链携带，而不是赖氨酸。这种精氨酸偏好可能是由于侧链胍基独特的水化性质，分子动力学模拟表明，这种性质有助于其通过封闭VSD中心的疏水塞子移动。为了测试这个模型中隐含的侧链相互作用，我们在蛋白质数据库中检查了精氨酸和赖氨酸的侧链与蛋白质中19种非甘氨酸氨基酸的相互作用。精氨酸胍与非极性芳香族和脂肪族侧链相互作用，而与极性侧链的氢键仅限于平面内位置。相反，非极性侧链主要与赖氨酸侧链的脂肪部分相互作用。在蛋白质结构和分子动力学模拟中，精氨酸和赖氨酸的水化特性强烈地反映在它们与非极性和极性侧链的相互作用中，这可能是精氨酸在VSD中作为移动电荷载体的偏好的基础。
Gating charges in voltage-sensing domains (VSD) of voltage-sensitive ion channels and enzymes are carried on arginine side chains rather than lysine. This arginine preference may result from the unique hydration properties of the side chain guanidinium group which facilitates its movement through a hydrophobic plug that seals the center of the VSD, as suggested by molecular dynamics simulations. To test for side chain interactions implicit in this model we inspected interactions of the side chains of arginine and lysine with each of the 19 non-glycine amino acids in proteins in the protein data bank. The arginine guanidinium interacts with non-polar aromatic and aliphatic side chains above and below the guanidinium plane while hydrogen bonding with polar side chains is restricted to in-plane positions. In contrast, non-polar side chains interact largely with the aliphatic part of the lysine side chain. The hydration properties of arginine and lysine are strongly reflected in their respective interactions with non-polar and polar side chains as observed in protein structures and in molecular dynamics simulations, and likely underlie the preference for arginine as a mobile charge carrier in VSD.
影响因子：
3.4
作者：
Colenso, Charlotte K.;Cao, Yang;Sessions, Richard B.;Hancox, Jules C.;Dempsey, Christopher E.
通讯作者：
Dempsey, Christopher E.