Transmembrane helix assembly and the role of salt bridges.
Transmembrane helix assembly and the role of salt bridges.
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DOI：
10.1016/j.sbi.2014.05.003
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发表时间：
2014-08
影响因子：
6.8
通讯作者：
Torsten H. Walther;A. Ulrich
中科院分区：
文献类型：
--
作者：
Torsten H. Walther;A. Ulrich
重点介绍了跨膜螺旋-螺旋相互作用基序的简要概述;跨膜片段通过局部盐桥的组装;膜中静电拉链的新概念;电荷拉链作为自然界和蛋白质工程的设计原则;跨膜螺旋-螺旋相互作用介导膜蛋白的折叠和组装。识别基序的范围从GxxxG和亮氨酸拉链到极性侧链和盐桥。一些典型的膜蛋白含有局部电荷簇，这些电荷簇对于折叠和功能是重要的，并且必须与通过易位子稳定插入到双层中相容。最近，静电“电荷拉链”已被描述为另一种组装模体。蛋白质序列表现出准对称的互补电荷模式，可以形成盐桥的延伸梯。这些片段可以可逆地插入膜中，甚至可以穿过膜转位。大自然在运输过程中使用电荷拉链，它们也可以用于设计细胞穿透载体。
HighlightsA brief overview of transmembrane helix–helix interaction motifs.Assembly of transmembrane segments via local salt bridges.A new concept of electrostatic charge zippers in membranes.Charge zippers as a design principle in nature and protein engineering.Transmembrane helix–helix interactions mediate the folding and assembly of membrane proteins. Recognition motifs range from GxxxG and leucine zippers to polar side chains and salt bridges. Some canonical membrane proteins contain local charge clusters that are important for folding and function, and which have to be compatible with a stable insertion into the bilayer via the translocon. Recently, the electrostatic “charge zipper” has been described as another kind of assembly motif. The protein sequences exhibit a quasi-symmetrical pattern of complementary charges that can form extended ladders of salt bridges. Such segments can insert reversibly into membranes, or even translocate across them. Nature uses charge zippers in transport processes, and they can also be adapted in the design of cell-penetrating carriers.