Aquaporin
From Proteopedia
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'''Aquaporins''' are channel producing proteins which regulate the flow of water across the cell membrane. More details of '''aquaporin-1''' in [[Aquaporin-1]]. '''Aquaglyceroporin''' (GLpf) conducts water and polyalcohols. The image on the left shows the protein, 6 molecules of glycerol and one of beta-octylglucoside. | '''Aquaporins''' are channel producing proteins which regulate the flow of water across the cell membrane. More details of '''aquaporin-1''' in [[Aquaporin-1]]. '''Aquaglyceroporin''' (GLpf) conducts water and polyalcohols. The image on the left shows the protein, 6 molecules of glycerol and one of beta-octylglucoside. | ||
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| + | == Disease == | ||
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| + | Mutations in aquaporin-2 cause diabitis insipidus. Mutations in aquaporin-0 in mice cause congenital cataracts. | ||
== Structural highlights == | == Structural highlights == | ||
| - | Aquaporins are made of α-helix bundles. | + | 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. |
== 3D Structures of Aquaporin == | == 3D Structures of Aquaporin == | ||
Revision as of 10:06, 3 November 2015
Contents |
Function
Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. More details of aquaporin-1 in Aquaporin-1. Aquaglyceroporin (GLpf) conducts water and polyalcohols. The image on the left shows the protein, 6 molecules of glycerol and one of beta-octylglucoside.
Disease
Mutations in aquaporin-2 cause diabitis insipidus. Mutations in aquaporin-0 in mice cause congenital cataracts.
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.
3D Structures of Aquaporin
Updated on 03-November-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Mark Leiserson, David Canner, Jaime Prilusky, Eran Hodis
