Walther Torsten H, Ulrich Anne S
Karlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG2) and Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany.
Karlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG2) and Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany.
Curr Opin Struct Biol. 2014 Aug;27:63-8. doi: 10.1016/j.sbi.2014.05.003. Epub 2014 Jun 5.
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.
跨膜螺旋-螺旋相互作用介导膜蛋白的折叠与组装。识别基序范围从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对折叠和功能很重要的局部电荷簇，并且这些电荷簇必须与通过转运体稳定插入双层膜兼容。最近，静电“电荷拉链”已被描述为另一种组装基序。蛋白质序列呈现出互补电荷的准对称模式，可形成延伸的盐桥梯。这样的片段可以可逆地插入膜中，甚至穿过膜进行转运。自然界在运输过程中使用电荷拉链，它们也可应用于细胞穿透载体的设计。
