Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 A resolution.
Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 A resolution.
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DOI：
10.1006/jmbi.1995.0444
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发表时间：
1995-08
影响因子：
5.6
通讯作者：
B. Jap;Huilin Li
中科院分区：
文献类型：
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作者：
B. Jap;Huilin Li
从牛红细胞膜中纯化并用脂质重建了一种由α-葡萄糖调节的H2O-通道，水通道蛋白-CHIP，形成了分辨率为约3.0 A的二维结晶斑块。记录嵌入葡萄糖中的晶体片的电子衍射图案和高分辨率图像，并用于计算3.5 A分辨率的投影图。该图谱证实了由α-葡萄糖调节的H2O通道基本包装单元是一个四聚体，并开始揭示其结构设计。H2O通道蛋白的基本结构由一个类似于梯形的包膜和一个位于梯形内的亚结构组成，该亚结构在通道结构本身中起着至关重要的作用;在该亚结构附近有一个密度非常低的区域，这是通道的可能位置。类椭圆形的包膜由高密度区域组成，其中许多可以解释为α-螺旋沿着其轴的投影。
An osmo-regulated H2O-channel, aquaporin-CHIP, from bovine red blood cell membranes was purified and reconstituted with lipids, forming two-dimensional crystalline patches that diffract to about 3.0 A resolution. Electron diffraction patterns and high-resolution images of the crystalline patches embedded in glucose were recorded and used to calculate the projection map at 3.5 A resolution. The map confirms that the osmo-regulated H2O-channel basic packing unit is a tetramer and begins to reveal it's structural design. The basic architecture of the H2O-channel protein consists of a trapezoid-like envelope and a substructure located within the trapezoid that could play a crucial role in the channel structure itself; near this substructure there is a region of very low density, which is the probable site of the channel. The trapezoid-like envelope is composed of high density regions many of which can be interpreted as projections of alpha-helices along their axes.