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  Structure and function of water channels

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F357-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E4A2-9
Genre: Journal Article

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16638.pdf (Publisher version), 0B
 
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Fujiyoshi, Y., Author
Mitsuoka, K., Author
de Groot, B. L.1, Author
Philippsen, A., Author
Grubmueller, H.1, Author
Agre, P., Author
Engel, A., Author
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1Max Planck Society, ou_persistent13              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2002-08
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Current Opinion in Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 12 (4) Sequence Number: - Start / End Page: 509 - 515 Identifier: -