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The 4.5 A structure of human AQP2

Schenk, Andreas D. and Werten, Paul J. L. and Scheuring, Simon and de Groot, Bert L. and Müller, Shirley A. and Stahlberg, Henning and Philippsen, Ansgar and Engel, Andreas. (2005) The 4.5 A structure of human AQP2. Journal of molecular biology, Vol. 350, H. 2. pp. 278-289.

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Official URL: http://edoc.unibas.ch/dok/A5257638

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0022-2836
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:55
Deposited On:08 Jun 2012 06:45

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