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Journal Article

Structure and function of water channels


de Groot,  B. L.
Max Planck Society;

Grubmueller,  H.
Max Planck Society;

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Fujiyoshi, Y., Mitsuoka, K., de Groot, B. L., Philippsen, A., Grubmueller, H., Agre, P., et al. (2002). Structure and function of water channels. Current Opinion in Structural Biology, 12(4), 509-515. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VS6-46FMK21-H-7&_cdi=6254&_user=38661&_pii=S0959440X0200355X&_origin=search&_coverDate=08%2F01%2F2002&_sk=999879995&view=c&wchp=dGLzVlz-zSkWb&md5=55b08d278031061ccca445762df340eb&ie=/sdarticle.pdf.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F357-C
Aquaporins comprise a family of water-transporting membrane proteins. All aquaporins are efficient water transporters, while sustaining strict selectivity, even against protons, thereby maintaining the proton gradient across the cell membrane. Recently solved structures of these membrane channels have helped us to understand this remarkable property. The structure of the Escherichia coli glycerol facilitator GlpF at 2,2 A resolution has enabled the refinement of a low-resolution human aquaporin-1 structure. This latter structure has recently been confirmed by the 2.2 Angstrom structure of bovine aquaporin-1. Further insights, particularly with respect to the dynamics of water permeation and the filter mechanism, have come from recent molecular dynamics simulations.