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Structural determinants of water permeation through aquaporin-1.
National Institute for Physiological Sciences, Okazaki, Japan.
Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.
PMID: 11034202 [PubMed - indexed for MEDLINE]
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Cited by 98 PubMed Central articles
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Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.
Fischer G, Kosinska-Eriksson U, Aponte-Santamaría C, Palmgren M, Geijer C, Hedfalk K, Hohmann S, de Groot BL, Neutze R, Lindkvist-Petersson K.
PLoS Biol. 2009 Jun; 7(6):e1000130. Epub 2009 Jun 16.
[PLoS Biol. 2009]
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High-resolution x-ray structure of human aquaporin 5.
Horsefield R, Nordén K, Fellert M, Backmark A, Törnroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R.
Proc Natl Acad Sci U S A. 2008 Sep 9; 105(36):13327-32. Epub 2008 Sep 3.
[Proc Natl Acad Sci U S A. 2008]
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Heterologous expression and purification systems for structural proteomics of Mammalian membrane proteins.
Mus-Veteau I.
Comp Funct Genomics. 2002; 3(6):511-7.
[Comp Funct Genomics. 2002]
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Structures reported by this article