Aquaporin
From Proteopedia
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- | + | <StructureSection load='1h6i' size='350' side='right' scene='' caption='Human aquaporin 1, [[1h6i]]'> | |
== Function == | == Function == | ||
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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. | 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. | ||
- | + | </StructureSection> | |
== 3D Structures of Aquaporin == | == 3D Structures of Aquaporin == | ||
Revision as of 09:26, 8 December 2015
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3D Structures of Aquaporin
Updated on 08-December-2015
References
- ↑ Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 2003 Nov 27;555(1):72-8. PMID:14630322
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Michal Harel, Alexander Berchansky, Mark Leiserson, David Canner, Jaime Prilusky, Eran Hodis