Structural determinants of water permeation through aquaporin-1
Structural determinants of water permeation through aquaporin-1
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DOI：
10.1038/35036519
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发表时间：
2000-10-05
期刊：
影响因子：
64.8
通讯作者：
Fujiyoshi, Y
中科院分区：
文献类型：
--
作者：
Murata, K;Mitsuoka, K;Fujiyoshi, Y
人红细胞水通道蛋白1是第一个功能明确的水通道蛋白家族成员。在这里，我们描述了一个原子模型的AQP 1在3.8埃的分辨率从电子晶体学数据。多个高度保守的氨基酸残基稳定了AQP 1的新折叠。水通道排列有保守的疏水残基，其允许快速的水运输，而水选择性是由于在一个残基的跨度上孔径收缩至约3埃。原子模型为一个长期存在的生理学难题提供了一个可能的分子解释--细胞膜如何可以自由地渗透水，但却不能渗透质子。
Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8 Angstrom resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 Angstrom over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.