Aquaporin

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spinqualitylabelsall models PDB ID 3gd8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Human Aquaporin 4 complex with glycerol and β-octylglucoside, 3gd8
Ligands:	,
Gene:	AQP4 (Homo sapiens)
Structural annotation: Resources: InterPro : Ipr012269, Ipr000425 Pfam : PF00230 UniProt : P55087
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. They are made of α-helix bundles. Aquaglyceroporin (GLpf) conducts water and polyalcohols. The images at the left and at the right correspond to one representative aquaporin structure, i.e. the crystal structure of human Aquaporin 4 (3gd8). The image shows the protein, 6 molecules of glycerol and one of beta-octylglucoside.

3D Structures of Aquaporin

Aquaporin

3llq – Aqp – Agrobacterium tumefaciens
3cll, 3cn5, 3cn6 – sAqp SoPIP2 (mutant) – spinach
1z98, 2b5f - sAqp SoPIP2

Aquaporin 0

2c32, 1ymg, 2b6p – cAqp0 – cow
2b6o – Aqp0 - electron crystallography – sheep
1sor, 3m9i – Aqp0 – Ovis aries

Aquaporin 1

2w1p, 2w2e – Aqp1 – Pischia pastoris
1fqy – hAqp1 – electron crystallography - human
1h6i, 1ih5 – hAqp1
1j4n – cAqp1

Aquaporin 4

2zz9 – rAqp4 (mutant) – rat
2d57, 3iyz – rAqp4 – electron crystallography
3gd8 – hAqp4 – human

Aquaporin 5

3d9s – hAqp5

Aquaporin M

2evu, 2f2b – AqpM – Methanothermobacter marburgensis

Aquaporin Z

2o9d, 2o9f, 3nk5, 3nka, 3nkc – EcAqpZ (mutant) – Escherichia coli
2o9e, 2o9g - EcAqpZ (mutant)+Hg
2abm, 1rc2 - EcAqpZ

3D Structures of Aquaglyceroporin

1lda, 1ldi – EcGLpf
1ldf – EcGLpf (mutant)
3c02 – GLpf – Plasmodium falciparum

References

1. Crane, J.M., Tajima, M., and Verkman, A.S. Live-cell imaging of aquaporin-4 diffusion and interactions in orthogonal arrays of particles. Neuroscience (2010) vol. 168 (4) pp. 892-902
2. Hiroaki, Y., Tani, K., Kamegawa, A., Gyobu, N., Nishikawa, K., Suzuki, H., Walz, T., Sasaki, S., Mitsuoka, Kimura, K., Mizoguchi, A., and Fujiyoshi, Y. Implications of the aquaporin-4 structure on array formation and cell adhesion. J Mol Biol (2006) vol. 355 (4) pp. 628-39
3. Nicchia, G.P., Rossi, A., Mola, M.G., Pisani, F., Stigliano, C., Basco, D., Mastrototaro, M., Svelto, M., and A. Frigeri. Higher order structure of aquaporin-4. Neuroscience (2010) vol. 168 (4) pp. 903-14
4. Pittock SJ, and Lennon V.A. Aquaporin-4 autoantibodies in a paraneoplastic context. Arch Neurol (2008) 65:629–632.
5. Hinson, S.R., McKeon, A., and Lennon V.A. Neurological autoimmunity targeting aquaporin-4. Neuroscience (2010) vol. 168 (4) pp. 1009-18.
6. Saadoun S., Papadopoulos M.C., Hara-Chikuma M, Verkman A.S. Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption. Nature (2005) 434:786–792.
7. Verkman A.S., Hara-Chikuma M., Papadopoulos M.C. Aquaporins—new players in cancer biology. J Mol Med (2008) 86:523–529.