The importance of aquaporin water channel protein structures

被引:113
作者
Engel, A [1 ]
Fijiyoshi, Y
Agre, P
机构
[1] Univ Basel, ME Muller Inst Microscopy, Biozentrum, CH-4056 Basel, Switzerland
[2] Kyoto Univ, Fac Sci, Dept Biophys, Sakyo Ku, Kyoto 60601, Japan
[3] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
[4] Johns Hopkins Univ, Sch Med, Dept Med, Baltimore, MD 21205 USA
关键词
aquaporins; atomic force microscopy; electron crystallography; electron microscopy;
D O I
10.1093/emboj/19.5.800
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The history of the water channel and recent structural and functional analyses of aquaporins are reviewed, These ubiquitous channels are important for bacteria, plants and animals, exhibit a pronounced sequence homology and share functional as well as structural similarities. Aquaporins allow water or small specific solutes to pass unhindered, but black the passage of ions to prevent dissipation of the transmembrane potential. Besides advances in structure determination, recent experiments suggest that many of these channels are regulated by pH variations, phosphorylation and binding of auxiliary proteins.
引用
收藏
页码:800 / 806
页数:7
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