Three-dimensional organization of a human water channel

Anchi Cheng, A. N. van Hoek, M. Yeager, A. S. Verkman and A. K. Mitra ()
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Anchi Cheng: The Scripps Research Institute
A. N. van Hoek: The Scripps Research Institute
M. Yeager: The Scripps Research Institute
A. S. Verkman: University of California, San Francisco
A. K. Mitra: The Scripps Research Institute

Nature, 1997, vol. 387, issue 6633, 627-630

Abstract: Abstract Aquaporins (AQP) are members of the major intrinsic protein (MIP) superfamily of integral membrane proteins and facilitate water transport in various eukaryotes and prokaryotes1,2. The archetypal aquaporin AQP1 is a partly glycosylated water-selective channel3,4 that is widely expressed in the plasma membranes of several water-permeable epithelial and endothelial cells2,5. Here we report the three-dimensional structure of deglycosylated, human erythrocyte AQP1, determined at 7Å resolution in the membrane plane by electron crystallography of frozen-hydrated two-dimensional crystals6,7. The structure has an in-plane, intramolecular 2-fold axis of symmetry located in the hydrophobic core of the bilayer. The AQP1 monomer is composed of six membrane-spanning, tilted α-helices. These helices form a barrel that encloses a vestibular region leading to the water-selective channel, which is outlined by densities attributed to the functionally important NPA boxes8 and their bridges to the surrounding helices. The intramolecular symmetry within the AQP1 molecule represents a new motif for the topology and design of membrane protein channels, and is a simple and elegant solution to the problem of bidirectional transport across the bilayer.

Date: 1997
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DOI: 10.1038/42517

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