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

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

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

dc.contributor.author	Walz, Thomas
dc.contributor.author	Harrison, Stephen
dc.contributor.author	Fujiyoshi, Yoshinori
dc.contributor.author	Hiroaki, Yoko
dc.contributor.author	Sliz, Piotr
dc.contributor.author	Cheng, Yifan
dc.contributor.author	Gonen, Tamir
dc.date.accessioned	2011-02-09T19:30:29Z
dc.date.issued	2005
dc.identifier.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.	en
dc.identifier.issn	0028-0836	en
dc.identifier.uri	http://nrs.harvard.edu/urn-3:HUL.InstRepos:4723671
dc.description.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.	en
dc.description.sponsorship	Molecular and Cellular Biology	en
dc.language.iso	en_US	en
dc.publisher	Nature Publishing Group	en
dc.relation.isversionof	http://dx.doi.org/10.1038/nature04321	en
dc.relation.hasversion	http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1350984&blobtype=pdf	en
dash.license	LAA
dc.subject	electron crystallography	en
dc.subject	lipid-protein interaction	en
dc.subject	two-dimensional crystal	en
dc.subject	MIP	en
dc.subject	lens	en
dc.subject	aquaporin-0	en
dc.title	Lipid-Protein Interactions in Double-Layered Two-Dimensional AQP0 Crystals	en
dc.relation.journal	Nature	en
dash.depositing.author	Harrison, Stephen
dc.date.available	2011-02-09T19:30:29Z