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='' 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.
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</StructureSection>
== 3D Structures of Aquaporin ==
== 3D Structures of Aquaporin ==

Revision as of 09:26, 8 December 2015

Human aquaporin 1, 1h6i

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3D Structures of Aquaporin

Updated on 08-December-2015


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
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