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          Institute: MPI für biophysikalische Chemie     Collection: Theoretische und computergestützte Biophysik (Dr. Helmut Grubmüller)     Display Documents



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ID: 16638.0, MPI für biophysikalische Chemie / Theoretische und computergestützte Biophysik (Dr. Helmut Grubmüller)
Structure and function of water channels
Authors:Fujiyoshi, Y.; Mitsuoka, K.; de Groot, B. L.; Philippsen, A.; Grubmueller, H.; Agre, P.; Engel, A.
Language:English
Date of Publication (YYYY-MM-DD):2002-08
Title of Journal:Current Opinion in Structural Biology
Volume:12
Issue / Number:4
Start Page:509
End Page:515
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Comment of the Author/Creator:Date: 2002, AUG
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Helmut Grubmüller / 070
MPI für biophysikalische Chemie/AG Bert de Groot
External Affiliations:Kyoto Univ, Fac Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502,; Japan; Biol Informat Res Ctr, Tokyo 1350064, Japan; Univ Basel, ME Muller Inst Microscopy, Biozentrum, CH-4056 Basel, Switzerland; Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
Identifiers:URL:http://www.sciencedirect.com/science?_ob=MImg&_ima...
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