The 4.5 A structure of human AQP2. Academic Article uri icon

Overview

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.

publication date

  • July 8, 2005

Research

keywords

  • Aquaporins

Identity

Scopus Document Identifier

  • 20444420877

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2005.04.030

PubMed ID

  • 15922355

Additional Document Info

volume

  • 350

issue

  • 2