Aquaporin

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{{STRUCTURE_1h6i| PDB=1h6i | SIZE=350| SCENE= |right|CAPTION=Human aquaporin 1, [[1h6i]] }}
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<StructureSection load='1h6i' size='350' side='right' scene='41/411407/Cv/3' caption='Human aquaporin 1, [[1h6i]]'>
== Function ==
== Function ==
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'''Aquaporins''' are channel producing proteins which regulate the flow of water across the cell membrane. The image on the left shows the protein, 6 molecules of glycerol and one of beta-octylglucoside.<br />
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'''Aquaporins''' are channel producing proteins which regulate the flow of water across the cell membrane.<ref>PMID:14630322</ref><br />
*'''Aquaporin-0''' functions as water channel in lens fibers.<br />
*'''Aquaporin-0''' functions as water channel in lens fibers.<br />
*'''Aquaporin-1''' see details in [[Aquaporin-1]].<br />
*'''Aquaporin-1''' see details in [[Aquaporin-1]].<br />
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*'''Aquaporin-4''' regulates water balance in the central nervous system.<br />
*'''Aquaporin-4''' regulates water balance in the central nervous system.<br />
*'''Aquaporin-5''' is implicated in the forming of saliva, tears and pulmonary secretions.<br />
*'''Aquaporin-5''' is implicated in the forming of saliva, tears and pulmonary secretions.<br />
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*'''Aquaporin-7''' regulates nutrient availability and signaling responding to cellular stress<ref>PMID:32631905</ref>
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*'''Aquaporin-10''' is expressed exclusively in adipocytes and participates in maintaining low glycerol content in them<ref>PMID:23382902</ref>
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*'''NIP-2 aquaporin''' Nodulin 26-like intrinsic protein is a plant Aquaporin<ref>PMID:34890456</ref>
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*'''TIP-2 aquaporin''' is permeable to water and ammonia<ref>PMID:29445244</ref>
*'''Aquaporin-Z''' is a major water channel in bacteria.<br />
*'''Aquaporin-Z''' is a major water channel in bacteria.<br />
*'''Aquaglycerolporin''' (GLpf) is a water channel which can transport glycerol, polyalcohols, urea and other small solutes.<br />
*'''Aquaglycerolporin''' (GLpf) is a water channel which can transport glycerol, polyalcohols, urea and other small solutes.<br />
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== Structural highlights ==
== Structural highlights ==
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Aquaporins are made of α-helix bundles. The water transporting channel contains 2 restriction sites conferring an hourglass model to the channel. Two NPA motifs from opposite surfaces form one restriction. Another restriction is formed by a cluster of aromatic/arginine side chains which serves to weaken the hydrogen bonding between water molecules.
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<scene name='41/411407/Cv/4'>Aquaporins are made of α-helix bundles</scene>. The water transporting channel contains 2 restriction sites conferring an hourglass model to the channel. Two NPA motifs from opposite surfaces form one restriction. Another restriction is formed by a cluster of aromatic/arginine side chains which serves to weaken the hydrogen bonding between water molecules.
== 3D Structures of Aquaporin ==
== 3D Structures of Aquaporin ==
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[[Aquaporin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Aquaporin
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==References==
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<references/>
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**[[3llq]] – Aqp – ''Agrobacterium tumefaciens''<br />
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**[[3cll]], [[3cn5]], [[3cn6]] – sAqp SoPIP2 (mutant) – spinach<br />
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**[[1z98]], [[2b5f]], [[4ia4]], [[4jc6]] - sAqp SoPIP2<br />
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**[[3zoj]] – Aqp PIP2-7 – ''Komagataella pastoris''<br />
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*Aquaporin 0
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**[[2c32]], [[1ymg]], [[2b6p]] – cAqp0 – cow<br />
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**[[2b6o]] – Aqp0 - electron crystallography – sheep<br />
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**[[1sor]], [[3m9i]] – Aqp0 – ''Ovis aries''
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*Aquaporin 1
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**[[2w1p]], [[2w2e]] – Aqp1 – ''Pischia pastoris''<br />
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**[[1fqy]] – hAqp1 – electron crystallography - human<br />
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**[[1h6i]], [[1ih5]], [[4csk]] – hAqp1<br />
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**[[1j4n]] – cAqp1<br />
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* Aquaporin 2
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**[[4csk]] – hAqp2<br />
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**[[4oj2]] – hAqp2 (mutant)<br />
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*Aquaporin 4
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**[[2zz9]] – rAqp4 (mutant) – rat<br />
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**[[2d57]], [[3iyz]] – rAqp4 – electron crystallography<br />
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**[[3gd8]] – hAqp4 – human<br />
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*Aquaporin 5
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**[[3d9s]] – hAqp5<br />
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*Aquaporin M
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**[[2evu]], [[2f2b]] – AqpM – ''Methanothermobacter marburgensis''<br />
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*Aquaporin Z
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**[[2o9d]], [[2o9f]], [[3nk5]], [[3nka]], [[3nkc]] – EcAqpZ (mutant) – ''Escherichia coli''<br />
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**[[2o9e]], [[2o9g]] - EcAqpZ (mutant)+Hg<br />
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**[[2abm]], [[1rc2]] - EcAqpZ<br />
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*Aquaglyceroporin
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**[[1lda]], [[1ldi]] – EcGLpf<br />
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**[[1ldf]] – EcGLpf (mutant)<br />
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**[[3c02]] – GLpf – ''Plasmodium falciparum''<br />
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**[[1fx8]] – EcGLpf + glycerol<br />
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}}
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human aquaporin 1, 1h6i

Drag the structure with the mouse to rotate

References

  1. ↑ Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 2003 Nov 27;555(1):72-8. PMID:14630322
  2. ↑ Dai C, Charlestin V, Wang M, Walker ZT, Miranda-Vergara MC, Facchine BA, Wu J, Kaliney WJ, Dovichi NJ, Li J, Littlepage LE. Aquaporin-7 Regulates the Response to Cellular Stress in Breast Cancer. Cancer Res. 2020 Oct 1;80(19):4071-4086. PMID:32631905 doi:10.1158/0008-5472.CAN-19-2269
  3. ↑ Laforenza U, Scaffino MF, Gastaldi G. Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. PLoS One. 2013;8(1):e54474. PMID:23382902 doi:10.1371/journal.pone.0054474
  4. ↑ Beamer ZG, Routray P, Choi WG, Spangler MK, Lokdarshi A, Roberts DM. Aquaporin family lactic acid channel NIP2;1 promotes plant survival under low oxygen stress in Arabidopsis. Plant Physiol. 2021 Dec 4;187(4):2262-2278. PMID:34890456 doi:10.1093/plphys/kiab196
  5. ↑ Lindahl V, Gourdon P, Andersson M, Hess B. Permeability and ammonia selectivity in aquaporin TIP2;1: linking structure to function. Sci Rep. 2018 Feb 14;8(1):2995. PMID:29445244 doi:10.1038/s41598-018-21357-2
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