Lipid-Protein Interactions in Double-Layered Two-Dimensional AQP0 Crystals

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Lipid-Protein Interactions in Double-Layered Two-Dimensional AQP0 Crystals

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Title: Lipid-Protein Interactions in Double-Layered Two-Dimensional AQP0 Crystals
Author: Walz, Thomas; Harrison, Stephen; Fujiyoshi, Yoshinori; Hiroaki, Yoko; Sliz, Piotr; Cheng, Yifan; Gonen, Tamir

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Citation: Gonen, Tamir, Yifan Cheng, Piotr Sliz, Yoko Hiroaki, Yoshinori Fujiyoshi, Stephen C. Harrison, and Thomas Walz. 2005. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438, no. 7068: 633-638.
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Abstract: Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. We describe a 1.9 Å resolution structure of junctional AQP0, determined by electron crystallography of double-layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic N- and C-termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We could therefore build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid-protein interactions.
Published Version: http://dx.doi.org/10.1038/nature04321
Other Sources: http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1350984&blobtype=pdf
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4723671

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  • FAS Scholarly Articles [7594]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
 
 

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