The 4.5 A structure of human AQP2.

Details

Serval ID
serval:BIB_C48AEB74B792
Type
Article: article from journal or magazin.
Collection
Publications
Title
The 4.5 A structure of human AQP2.
Journal
Journal of molecular biology
Author(s)
Schenk A.D., Werten P.J., Scheuring S., de Groot B.L., Müller S.A., Stahlberg H., Philippsen A., Engel A.
ISSN
0022-2836 (Print)
ISSN-L
0022-2836
Publication state
Published
Issued date
08/07/2005
Peer-reviewed
Oui
Volume
350
Number
2
Pages
278-289
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Located in the principal cells of the collecting duct, aquaporin-2 (AQP2) is responsible for the regulated water reabsorption in the kidney and is indispensable for the maintenance of body water balance. Disregulation or malfunctioning of AQP2 can lead to severe diseases such as nephrogenic diabetes insipidus, congestive heart failure, liver cirrhosis and pre-eclampsia. Here we present the crystallization of recombinantly expressed human AQP2 into two-dimensional protein-lipid arrays and their structural characterization by atomic force microscopy and electron crystallography. These crystals are double-layered sheets that have a diameter of up to 30 microm, diffract to 3 A(-1) and are stacked by contacts between their cytosolic surfaces. The structure determined to 4.5 A resolution in the plane of the membrane reveals the typical aquaporin fold but also a particular structure between the stacked layers that is likely to be related to the cytosolic N and C termini.
Keywords
Aquaporin 2, Aquaporins/chemistry, Aquaporins/ultrastructure, Cryoelectron Microscopy, Crystallization, Humans, Microscopy, Atomic Force, Microscopy, Electron, Scanning Transmission, Microscopy, Electron, Transmission
Pubmed
Web of science
Create date
30/06/2023 10:07
Last modification date
28/07/2023 6:59
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