The structure of aquaporins

  title={The structure of aquaporins},
  author={Tamir Gonen and Thomas Walz},
  journal={Quarterly Reviews of Biophysics},
  pages={361 - 396}
  • T. Gonen, T. Walz
  • Published 1 November 2006
  • Biology
  • Quarterly Reviews of Biophysics
1. Introduction 362 1.1 The elusive water pores 362 1.2 CHIP28 362 2. Studies on AQP-1 363 2.1 Expression of AQP1 cDNA in Xenopus oocytes 363 2.2 Reconstitution of purified AQP1 into artificial lipid bilayers 364 2.3 Structural information deduced from the primary sequence 365 2.4 Evolution and mammalian AQPs 365 3. Chronological overview over AQP structures 368 3.1 AQP1 – the red blood cell water pore 368 3.2 GlpF – the E. coli glycerol facilitator 371 3.3 AQPZ – the E. coli water pore 372 3.4… 
1,3‐propanediol binds deep inside the channel to inhibit water permeation through aquaporins
It is predicted that PDO can be an effective diuretic which directly modulates water flow through the protein channels and should be free from the serious side effects associated with other diuretics that change the hydro‐homeostasis indirectly by altering the osmotic gradients.
Aquaporin-7: A Dynamic Aquaglyceroporin With Greater Water and Glycerol Permeability Than Its Bacterial Homolog GlpF
Xenopus oocytes expressing human aquaporin-7 (AQP7) exhibit greater osmotic water permeability and 3H-glycerol uptake vs. those expressing the bacterial glycerol facilitator GlpF, and X-ray crystallographic structure determination of AQP7 and molecular-dynamics simulations demonstrate that F74 undergoes large and rapid conformational changes, allowing glycerols molecules to permeate without orientational restriction.
In silico study of human aquaporin AQP11 and AQP12 channels
This analysis points out a possible alternative ar/R site and shows that these aquaporins feature unique residues at key pore‐lining positions that make the shape, composition and electrostatics of their channel peculiar.
1,3-Propanediol binds inside the water-conducting pore of aquaporin 4: Does this efficacious inhibitor have sufficient potency?
1,3-propanediol is predicted to be an effective drug for brain edema and other AQP4-correlated neurological conditions because of the fact that PDO is classified by the US Food and Drug Administration as generally safe.
Molecular dynamics study of the archaeal aquaporin AqpM
MD simulations of AqpM extend previous evidence that this archaeal aquaporin exhibits hybrid features intermediate between the two known Aquaporin sub-families, supporting the idea that it may constitute a member of a novel class of aquaporins.
Functional characterization of aquaporins and aquaglyceroporins of the yellow fever mosquito, Aedes aegypti
It is found that AQPs are generally down-regulated 24 hrs after a blood meal, and Malpighian tubules of adult female yellow fever mosquitoes utilize three distinct AQPs and one aquaglyceroporin in their osmoregulatory functions.
Invertebrate aquaporins: a review
The physiological role of AQPs in invertebrates (insects, ticks and nematodes) is discussed, including their function in common invertebrate phenomena such as high-volume liquid diets, cryoprotection and anhydrobiosis.
Identification of Aquaporin 1 in Diplodus sargus
Although the structure of the AQP protein in different species is conserved, results showed that the S. aurata and D. sargus AQP-1 proteins have evolved similarly.


The channel architecture of aquaporin 0 at a 2.2-A resolution.
The structure of this eukaryotic, integral membrane protein suggests that the selectivity of AQP0 for water transport is based on the identity and location of signature amino acid residues that are hallmarks of the water-selective arm of the AQP family of proteins.
Transport of Water and Glycerol in Aquaporin 3 Is Gated by H+ *
Aquaporins were expressed in Xenopus laevis oocytes in order to study the effects of external pH and solute structure on permeabilities and it is suggested that water and polyols permeate AQP3 by forming successive hydrogen bonds with titratable sites.
The three-dimensional structure of aquaporin-1
A model that identifies the aqueous pore in the AQP1 molecule and indicates the organization of the tetrameric complex in the membrane is provided.
Characterization of Aquaporin-6 as a Nitrate Channel in Mammalian Cells
It is indicated that AQP6 exhibits a new form of anion permeation with marked specificity for nitrate conferred by a specific pore-lining residue, observations that imply that the primary role of AQP 6 may be in cellular regulation rather than simple fluid transport.
Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution.
It is proposed that the asparagine residue at the contact point between TM2 and TM5 in AQP6 may function as a teeter board needed for rapid structural oscillations during anion permeation.
Cellular and molecular biology of the aquaporin water channels.
The high water permeability characteristic of mammalian red cell membranes is now known to be caused by the protein AQP1, a tetramer with each subunit containing an aqueous pore likened to an hourglass formed by obversely arranged tandem repeats.
Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol.
A new member (AQP9) of the aquaporin family was identified from human leukocytes by homology cloning using PCR, suggesting a unique permeability character and may expand the understanding of water and small solute transport in the body.
Cloning and functional expression of a second new aquaporin abundantly expressed in testis.
The unexpected complexity of the presence of two aquaporins in testis may call for the further analysis of the role of aquaporin in the reproduction biology.
Cloning and Functional Expression of a New Water Channel Abundantly Expressed in the Testis Permeable to Water, Glycerol, and Urea*
A new member of the aquaporin (AQP) family has been identified from rat testis that encodes a 269-amino acid protein that contained the conserved NPA motifs of MIP family proteins.