Aquaporin
From Proteopedia
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| - | + | <StructureSection load='1h6i' size='350' side='right' scene='41/411407/Cv/3' caption='Human aquaporin 1, [[1h6i]]'> | |
== Function == | == Function == | ||
| - | '''Aquaporins''' are channel producing proteins which regulate the flow of water across the cell membrane. | + | '''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 /> | ||
| + | *'''Aquaporin-7''' regulates nutrient availability and signaling responding to cellular stress<ref>PMID:32631905</ref> | ||
| + | *'''Aquaporin-10''' is expressed exclusively in adipocytes and participates in maintaining low glycerol content in them<ref>PMID:23382902</ref> | ||
| + | *'''NIP-2 aquaporin''' Nodulin 26-like intrinsic protein is a plant Aquaporin<ref>PMID:34890456</ref> | ||
| + | *'''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 == | ||
| - | 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. | + | <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 == | ||
| + | [[Aquaporin 3D structures]] | ||
| - | + | </StructureSection> | |
| - | + | ||
| - | *Aquaporin | ||
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| - | **[[3llq]] – Aqp – ''Agrobacterium tumefaciens''<br /> | ||
| - | **[[3cll]], [[3cn5]], [[3cn6]] – sAqp SoPIP2 (mutant) – spinach<br /> | ||
| - | **[[1z98]], [[2b5f]], [[4ia4]], [[4jc6]] - sAqp SoPIP2<br /> | ||
| - | **[[3zoj]] – Aqp PIP2-7 – ''Komagataella pastoris''<br /> | ||
| - | |||
| - | *Aquaporin 0 | ||
| - | |||
| - | **[[2c32]], [[1ymg]], [[2b6p]] – cAqp0 – cow<br /> | ||
| - | **[[2b6o]] – Aqp0 - electron crystallography – sheep<br /> | ||
| - | **[[1sor]], [[3m9i]] – Aqp0 – ''Ovis aries'' | ||
| - | |||
| - | *Aquaporin 1 | ||
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| - | **[[2w1p]], [[2w2e]] – Aqp1 – ''Pischia pastoris''<br /> | ||
| - | **[[1fqy]] – hAqp1 – electron crystallography - human<br /> | ||
| - | **[[1h6i]], [[1ih5]], [[4csk]] – hAqp1<br /> | ||
| - | **[[1j4n]] – cAqp1<br /> | ||
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| - | * Aquaporin 2 | ||
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| - | **[[4csk]] – hAqp2<br /> | ||
| - | **[[4oj2]] – hAqp2 (mutant)<br /> | ||
| - | |||
| - | *Aquaporin 4 | ||
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| - | **[[2zz9]] – rAqp4 (mutant) – rat<br /> | ||
| - | **[[2d57]], [[3iyz]] – rAqp4 – electron crystallography<br /> | ||
| - | **[[3gd8]] – hAqp4 – human<br /> | ||
| - | |||
| - | *Aquaporin 5 | ||
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| - | **[[3d9s]] – hAqp5<br /> | ||
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| - | *Aquaporin M | ||
| - | |||
| - | **[[2evu]], [[2f2b]] – AqpM – ''Methanothermobacter marburgensis''<br /> | ||
| - | |||
| - | *Aquaporin Z | ||
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| - | **[[2o9d]], [[2o9f]], [[3nk5]], [[3nka]], [[3nkc]] – EcAqpZ (mutant) – ''Escherichia coli''<br /> | ||
| - | **[[2o9e]], [[2o9g]] - EcAqpZ (mutant)+Hg<br /> | ||
| - | **[[2abm]], [[1rc2]] - EcAqpZ<br /> | ||
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| - | *Aquaglyceroporin | ||
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| - | **[[1lda]], [[1ldi]] – EcGLpf<br /> | ||
| - | **[[1ldf]] – EcGLpf (mutant)<br /> | ||
| - | **[[3c02]] – GLpf – ''Plasmodium falciparum''<br /> | ||
| - | **[[1fx8]] – EcGLpf + glycerol<br /> | ||
| - | }} | ||
==References== | ==References== | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 2003 Nov 27;555(1):72-8. PMID:14630322
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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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