TY - JOUR
T1 - Structure and function of water channels
AU - Fujiyoshi, Yoshinori
AU - Mitsuoka, Kaoru
AU - De Groot, Bert L.
AU - Philippsen, Ansgar
AU - Grubmüller, Helmut
AU - Agre, Peter
AU - Engel, Andreas
N1 - Funding Information:
This work was supported by the Swiss National Foundation, the M. E. Müller-Foundation of Switzerland, the European Union-Quality of Life and Management of Living Resources Project (grant QLRT-2000-00778 and QLRT-2000/00504 to A. E.) and the Human Frontier Science Program (grant RG0021/2000-M103 to A. E.). B.L.d. G and H.G. were supported by the BIOTECH programs of the European Union (grants QLRT 2000/00778, and QLRT-2000/00504). P.A. was supported by grants from the National Institutes of Health. Y.F. was supported by Grant-in Aid for Specially Promoted Research (grant 13001003) and grants from Japan Biological Informatics Consortium.
PY - 2002/8/1
Y1 - 2002/8/1
N2 - Aquaporins comprise a family of water-transforming 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 Å resolution has enabled the refinement of a low-resolution human aquaporin-1 structure. This latter structure has recently been confirmed by the 2.2 Å 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.
AB - Aquaporins comprise a family of water-transforming 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 Å resolution has enabled the refinement of a low-resolution human aquaporin-1 structure. This latter structure has recently been confirmed by the 2.2 Å 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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U2 - 10.1016/S0959-440X(02)00355-X
DO - 10.1016/S0959-440X(02)00355-X
M3 - Review article
C2 - 12163075
AN - SCOPUS:0036667729
SN - 0959-440X
VL - 12
SP - 509
EP - 515
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -